CHI ELLEN (US)
EDWARDS WILSON (US)
LACOMBE ANN (US)
GREVING CARRIE (US)
LI XINYI (US)
LIN WAI (US)
What is claimed is: 1. An isolated monoclonal antibody or antigen binding fragment thereof that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:570, 571, and 572, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:573, 574, and 575, respectively; b. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:936, 937, and 938, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; c. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:918, 919, and 920, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:921, 922, and 923, respectively; d. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:900, 901, and 902, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:903, 904, and 905, respectively; e. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:276, 277, and 278, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:279, 280, and 281, respectively; f. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:294, 295, and 296, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:297, 298, and 299, respectively; g. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:318, 319, and 320, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:321, 322, and 323, respectively; h. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:324, 325, and 326, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:327, 328, and 329, respectively; i. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:330, 331, and 332, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:333, 334, and 335, respectively; j. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:342, 343, and 344, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:345, 346, and 347, respectively; k. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:354, 355, and 356, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:357, 358, and 359, respectively; l. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:360, 361, and 362, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:363, 364, and 365, respectively; m. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:366, 367, and 368, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:369, 370, and 371, respectively; n. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:384, 385, and 386, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:387, 388, and 389, respectively; o. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:906, 907, and 908, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:909, 910, and 911, respectively; p. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:420, 421, and 422, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:423, 424, and 425, respectively; q. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1026, 1027, and 1028, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1029, 1030, and 1031, respectively; r. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:912, 913, and 914, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:915, 916, and 917, respectively; s. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:426, 427, and 428, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:429, 430, and 431, respectively; t. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1194, 1195, and 1196, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1197, 1198, and 1199, respectively; u. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:438, 439, and 440, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:441, 442, and 443, respectively; v. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:444, 445, and 446, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:447, 448, and 449, respectively; w. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:456, 457, and 458, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:459, 460, and 461, respectively; x. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:462, 463, and 464, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:465, 466, and 467, respectively; y. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:468, 469, and 470, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:471, 472, and 473, respectively; z. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:474, 475, and 476, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:477, 478, and 479, respectively; aa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:480, 481, and 482, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:483, 484, and 485, respectively; bb. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:510, 511, and 512, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:513, 514, and 515, respectively; cc. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:528, 529, and 530, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:531, 532, and 533, respectively; dd. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:552, 553, and 554, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:555, 556, and 557, respectively; ee. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:558, 559, and 560, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:561, 562, and 563, respectively; ff. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:564, 565, and 566, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:567, 568, and 569, respectively; gg. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:576, 577, and 578, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:579, 580, and 581, respectively; hh. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:600, 601, and 602, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:603, 604, and 605, respectively; ii. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:606, 607, and 608, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:609, 610, and 611, respectively; jj. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:624, 625, and 626, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:627, 628, and 629, respectively; kk. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:642, 643, and 644, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:645, 646, and 647, respectively; ll. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:648, 649, and 650, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:651, 652, and 653, respectively; or mm. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:654, 655, and 656, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:657, 658, and 659, respectively. 2. The isolated monoclonal antibody or antigen binding fragment thereof of claim 1 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising the amino acid sequence of SEQ ID NO:236, and a VL comprising the amino acid sequence of SEQ ID NO:237; b. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; c. a VH comprising the amino acid sequence of SEQ ID NO:792, and a VL comprising the amino acid sequence of SEQ ID NO:793; d. a VH comprising the amino acid sequence of SEQ ID NO:786, and a VL comprising the amino acid sequence of SEQ ID NO:787; e. a VH comprising the amino acid sequence of SEQ ID NO:138, and a VL comprising the amino acid sequence of SEQ ID NO:139; f. a VH comprising the amino acid sequence of SEQ ID NO:144, and a VL comprising the amino acid sequence of SEQ ID NO:145; g. a VH comprising the amino acid sequence of SEQ ID NO:152, and a VL comprising the amino acid sequence of SEQ ID NO:153; h. a VH comprising the amino acid sequence of SEQ ID NO:154, and a VL comprising the amino acid sequence of SEQ ID NO:155; i. a VH comprising the amino acid sequence of SEQ ID NO:156, and a VL comprising the amino acid sequence of SEQ ID NO:157; j. a VH comprising the amino acid sequence of SEQ ID NO:160, and a VL comprising the amino acid sequence of SEQ ID NO:161; k. a VH comprising the amino acid sequence of SEQ ID NO:164, and a VL comprising the amino acid sequence of SEQ ID NO:165; l. a VH comprising the amino acid sequence of SEQ ID NO:166, and a VL comprising the amino acid sequence of SEQ ID NO:167; m. a VH comprising the amino acid sequence of SEQ ID NO:168, and a VL comprising the amino acid sequence of SEQ ID NO:169; n. a VH comprising the amino acid sequence of SEQ ID NO:174, and a VL comprising the amino acid sequence of SEQ ID NO:175; o. a VH comprising the amino acid sequence of SEQ ID NO:788, and a VL comprising the amino acid sequence of SEQ ID NO:789; p. a VH comprising the amino acid sequence of SEQ ID NO:186, and a VL comprising the amino acid sequence of SEQ ID NO:187; q. a VH comprising the amino acid sequence of SEQ ID NO:828, and a VL comprising the amino acid sequence of SEQ ID NO:829; r. a VH comprising the amino acid sequence of SEQ ID NO:790, and a VL comprising the amino acid sequence of SEQ ID NO:791; s. a VH comprising the amino acid sequence of SEQ ID NO:188, and a VL comprising the amino acid sequence of SEQ ID NO:189; t. a VH comprising the amino acid sequence of SEQ ID NO:884, and a VL comprising the amino acid sequence of SEQ ID NO:885; u. a VH comprising the amino acid sequence of SEQ ID NO:192, and a VL comprising the amino acid sequence of SEQ ID NO:193; v. a VH comprising the amino acid sequence of SEQ ID NO:194, and a VL comprising the amino acid sequence of SEQ ID NO:195; w. a VH comprising the amino acid sequence of SEQ ID NO:198, and a VL comprising the amino acid sequence of SEQ ID NO:199; x. a VH comprising the amino acid sequence of SEQ ID NO:200, and a VL comprising the amino acid sequence of SEQ ID NO:201; y. a VH comprising the amino acid sequence of SEQ ID NO:202, and a VL comprising the amino acid sequence of SEQ ID NO:203; z. a VH comprising the amino acid sequence of SEQ ID NO:204, and a VL comprising the amino acid sequence of SEQ ID NO:205; aa. a VH comprising the amino acid sequence of SEQ ID NO:206, and a VL comprising the amino acid sequence of SEQ ID NO:207; bb. a VH comprising the amino acid sequence of SEQ ID NO:216, and a VL comprising the amino acid sequence of SEQ ID NO:217; cc. a VH comprising the amino acid sequence of SEQ ID NO:222, and a VL comprising the amino acid sequence of SEQ ID NO:223; dd. a VH comprising the amino acid sequence of SEQ ID NO:230, and a VL comprising the amino acid sequence of SEQ ID NO:231; ee. a VH comprising the amino acid sequence of SEQ ID NO:232, and a VL comprising the amino acid sequence of SEQ ID NO:233; ff. a VH comprising the amino acid sequence of SEQ ID NO:234, and a VL comprising the amino acid sequence of SEQ ID NO:235; gg. a VH comprising the amino acid sequence of SEQ ID NO:238, and a VL comprising the amino acid sequence of SEQ ID NO:239; hh. a VH comprising the amino acid sequence of SEQ ID NO:246, and a VL comprising the amino acid sequence of SEQ ID NO:247; ii. a VH comprising the amino acid sequence of SEQ ID NO:248, and a VL comprising the amino acid sequence of SEQ ID NO:249; jj. a VH comprising the amino acid sequence of SEQ ID NO:254, and a VL comprising the amino acid sequence of SEQ ID NO:255; kk. a VH comprising the amino acid sequence of SEQ ID NO:260, and a VL comprising the amino acid sequence of SEQ ID NO:261; ll. a VH comprising the amino acid sequence of SEQ ID NO:262, and a VL comprising the amino acid sequence of SEQ ID NO:263; or mm. a VH comprising the amino acid sequence of SEQ ID NO:264, and a VL comprising the amino acid sequence of SEQ ID NO:265. 3. The isolated monoclonal antibody or antigen binding fragment thereof of claim 1 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:570, 571, and 572, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:573, 574, and 575, respectively; b. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:936, 937, and 938, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; c. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:918, 919, and 920, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:921, 922, and 923, respectively; d. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:900, 901, and 902, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:903, 904, and 905, respectively; or e. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:912, 913, and 914, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:915, 916, and 917, respectively. 4. The isolated monoclonal antibody or antigen binding fragment thereof of claim 2 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising the amino acid sequence of SEQ ID NO:236, and a VL comprising the amino acid sequence of SEQ ID NO:237; b. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; c. a VH comprising the amino acid sequence of SEQ ID NO:792, and a VL comprising the amino acid sequence of SEQ ID NO:793; d. a VH comprising the amino acid sequence of SEQ ID NO:786, and a VL comprising the amino acid sequence of SEQ ID NO:787; or e. a VH comprising the amino acid sequence of SEQ ID NO:790, and a VL comprising the amino acid sequence of SEQ ID NO:791. 5. The isolated monoclonal antibody or antigen binding fragment thereof of any of claims 1-4, wherein the mammalian cell is a human or rat cell. 6. The isolated monoclonal antibody or antigen binding fragment thereof of any of claims 1-5, wherein the cell is a primary immune cell. 7. An isolated monoclonal antibody or antigen binding fragment thereof which recognizes human and rat interleukin-23 receptor (IL-23R), wherein the antibody or fragment comprises: a. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:468, 469, and 470 , respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:471, 472, and 473, respectively; b. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:618, 619, and 620, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:621, 622, and 623, respectively; c. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:330, 331, and 332, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:333, 334, and 335, respectively; d. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:936,937, and 938, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; e. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:312, 313, and 314, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:315, 316, and 317, respectively; f. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:474, 475, and 476, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:477, 478, and 479, respectively; g. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:1194, 1195, and 1196, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1197, 1198, and 1199, respectively; h. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:426, 427, and 428, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:429, 430, and 431, respectively; or i. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:498, 499, and 500, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:501, 502, and 503, respectively. 8. The isolated monoclonal antibody or antigen binding fragment thereof of claim 7 which recognizes human and rat interleukin-23 receptor (IL-23R), wherein the antibody or fragment comprises: a. a VH comprising the amino acid sequence of SEQ ID NO:202, and a VL comprising the amino acid sequence of SEQ ID NO:203; b. a VH comprising the amino acid sequence of SEQ ID NO:252, and a VL comprising the amino acid sequence of SEQ ID NO:253; c. a VH comprising the amino acid sequence of SEQ ID NO:156, and a VL comprising the amino acid sequence of SEQ ID NO:157; d. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; e. a VH comprising the amino acid sequence of SEQ ID NO:150, and a VL comprising the amino acid sequence of SEQ ID NO:151; f. a VH comprising the amino acid sequence of SEQ ID NO:204, and a VL comprising the amino acid sequence of SEQ ID NO:205; g. a VH comprising the amino acid sequence of SEQ ID NO:884, and a VL comprising the amino acid sequence of SEQ ID NO:885; h. a VH comprising the amino acid sequence of SEQ ID NO:188, and a VL comprising the amino acid sequence of SEQ ID NO:189; or i. a VH comprising the amino acid sequence of SEQ ID NO:212, and a VL comprising the amino acid sequence of SEQ ID NO:213. 9. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1252, an LCDR2 SEQ ID NO:1253, and an LCDR3 SEQ ID NO:1254 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:900, an HCDR2 SEQ ID NO:901 and an HCDR3 SEQ ID NO:902; b. an HCDR1 SEQ ID NO:906, an HCDR2 SEQ ID NO:907, and an HCDR3 SEQ ID NO:908; c. an HCDR1 SEQ ID NO:912, an HCDR2 SEQ ID NO:913, and an HCDR3 SEQ ID NO:914; d. an HCDR1 SEQ ID NO:918, an HCDR2 SEQ ID NO:919, and an HCDR3 SEQ ID NO:920; e. an HCDR1 SEQ ID NO:942, an HCDR2 SEQ ID NO:943, and an HCDR3 SEQ ID NO:944; f. an HCDR1 SEQ ID NO:948, an HCDR2 SEQ ID NO:949, and an HCDR3 SEQ ID NO:950; g. an HCDR1 SEQ ID NO:1014, an HCDR2 SEQ ID NO:1015, and an HCDR3 SEQ ID NO:1016; h. an HCDR1 SEQ ID NO:1026, an HCDR2 SEQ ID NO:1027, and an HCDR3 SEQ ID NO:1028; and i. an HCDR1 SEQ ID NO:1152, an HCDR2 SEQ ID NO:1153, and an HCDR3 SEQ ID NO:1154. 10. The isolated monoclonal antibody or antigen binding fragment thereof of claim 9 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1252, an LCDR2 SEQ ID NO:1253, and an LCDR3 SEQ ID NO:1254 or having the amino acid sequence SEQ ID NO:1247 and a VH sequence selected from SEQ ID NO:786, 788, 790, 792, 800, 802, 824, 828 and 870. 11. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1255, an LCDR2 SEQ ID NO:1256, and an LCDR3 SEQ ID NO:1257 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:924, an HCDR2 SEQ ID NO:925, and an HCDR3 SEQ ID NO:926; b. an HCDR1 SEQ ID NO:1002, an HCDR2 SEQ ID NO:1003, and an HCDR3 SEQ ID NO:1004; c. an HCDR1 SEQ ID NO:1032, an HCDR2 SEQ ID NO:1033, and an HCDR3 SEQ ID NO:1034; d. an HCDR1 SEQ ID NO:1044, an HCDR2 SEQ ID NO:1045, and an HCDR3 SEQ ID NO:1046; e. an HCDR1 SEQ ID NO:1050, an HCDR2 SEQ ID NO:1051, and an HCDR3 SEQ ID NO:1052; f. an HCDR1 SEQ ID NO:1056, an HCDR2 SEQ ID NO:1057, and an HCDR3 SEQ ID NO:1058; g. an HCDR1 SEQ ID NO:1062, an HCDR2 SEQ ID NO:1063, and an HCDR3 SEQ ID NO:1064; h. an HCDR1 SEQ ID NO:1068, an HCDR2 SEQ ID NO:1069, and an HCDR3 SEQ ID NO:1070; i. an HCDR1 SEQ ID NO:1080, an HCDR2 SEQ ID NO:1081, and an HCDR3 SEQ ID NO:1082; j. an HCDR1 SEQ ID NO:1092, an HCDR2 SEQ ID NO:1093, and an HCDR3 SEQ ID NO:1094; k. an HCDR1 SEQ ID NO:1098, an HCDR2 SEQ ID NO:1099, and an HCDR3 SEQ ID NO:1100; l. an HCDR1 SEQ ID NO:1110, an HCDR2 SEQ ID NO:1111, and an HCDR3 SEQ ID NO:1112; m. an HCDR1 SEQ ID NO:1122, an HCDR2 SEQ ID NO:1123, and an HCDR3 SEQ ID NO:1124; n. an HCDR1 SEQ ID NO:1140, an HCDR2 SEQ ID NO:1141, and an HCDR3 SEQ ID NO:1142; o. an HCDR1 SEQ ID NO:1146, an HCDR2 SEQ ID NO:1147, and an HCDR3 SEQ ID NO:1148; and p. an HCDR1 SEQ ID NO:1158, an HCDR2 SEQ ID NO:1159, and an HCDR3 SEQ ID NO:1160. 12. The isolated monoclonal antibody or antigen binding fragment thereof of claim 11 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1255, an LCDR2 SEQ ID NO:1256, and an LCDR3 SEQ ID NO:1257 or having the amino acid sequence SEQ ID NO:1248 and a VH sequence selected from SEQ ID NO:794, 820, 830, 834, 836, 838, 840, 842, 846, 850, 852, 856, 860, 866, 868 and 872. 13. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1258, an LCDR2 SEQ ID NO:1259, and an LCDR3 SEQ ID NO:1260 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:930, an HCDR2 SEQ ID NO:931, and an HCDR3 SEQ ID NO:932; or b. an HCDR1 SEQ ID NO:954, an HCDR2 SEQ ID NO:955, and an HCDR3 SEQ ID NO:956. 14. The isolated monoclonal antibody or antigen binding fragment thereof of claim 13 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1258, an LCDR2 SEQ ID NO:1259, and an LCDR3 SEQ ID NO:1260 or a VL having the amino acid sequence SEQ ID NO:1249; and a VH sequence selected from SEQ ID NO:796 and 804. 15. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1261, an LCDR2 SEQ ID NO:1262, and an LCDR3 SEQ ID NO:1263 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:960, an HCDR2 SEQ ID NO:961, and an HCDR3 SEQ ID NO:962; and b. an HCDR1 SEQ ID NO:1182, an HCDR2 SEQ ID NO:1183, and an HCDR3 SEQ ID NO:1184. 16. The isolated monoclonal antibody or antigen binding fragment thereof of claim 15 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1261, an LCDR2 SEQ ID NO:1262, and an LCDR3 SEQ ID NO:1263 or a VL having the amino acid sequence SEQ ID NO:1250; and a VH sequence selected from SEQ ID NO:806 and 880. 17. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1264, an LCDR2 SEQ ID NO:1265, and an LCDR3 SEQ ID NO:1266 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:1008, an HCDR2 SEQ ID NO:1009, and an HCDR3 SEQ ID NO:1010; b. an HCDR1 SEQ ID NO:1020, an HCDR2 SEQ ID NO:1021, and an HCDR3 SEQ ID NO:1022; c. an HCDR1 SEQ ID NO:1038, an HCDR2 SEQ ID NO:1039, and an HCDR3 SEQ ID NO:1040; d. an HCDR1 SEQ ID NO:1074, an HCDR2 SEQ ID NO:1075, and an HCDR3 SEQ ID NO:1076; e. an HCDR1 SEQ ID NO:1086, an HCDR2 SEQ ID NO:1087, and an HCDR3 SEQ ID NO:1088; f. an HCDR1 SEQ ID NO:1104, an HCDR2 SEQ ID NO:1105, and an HCDR3 SEQ ID NO:1106; g. an HCDR1 SEQ ID NO:1128, an HCDR2 SEQ ID NO:1129, and an HCDR3 SEQ ID NO:1130; and h. an HCDR1 SEQ ID NO:1134, an HCDR2 SEQ ID NO:1135, and an HCDR3 SEQ ID NO:1136. 18. The isolated monoclonal antibody or antigen binding fragment thereof of claim 17 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1264, an LCDR2 SEQ ID NO:1265, and an LCDR3 SEQ ID NO:1266 or having the amino acid sequence SEQ ID NO:1251 and a VH sequence selected from SEQ ID NO: 806 and 880822, 826, 832, 844, 848, 854, 862 and 864. 19. A VHH antibody or nanobody that binds interleukin-23 receptor (IL-23R) comprising a VH sequence selected from SEQ ID NO:786, 788, 790, 792, 800, 802, 824, 828, 870, 794, 820, 830, 834, 836, 838, 840, 842, 846, 850, 852, 856, 860, 866, 868, 872, 796, 804, 806, 880, 822, 826, 832, 844, 848, 854, 862 or 864. 20. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising: a. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:276, 277, and 278, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:279, 280, and 281, respectively; b. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:288, 289, and 290, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:291, 292, and 293, respectively; c. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:294, 295, and 296, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:297, 298, and 299, respectively; d. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:306, 307, and 308, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:309, 310, and 311, respectively; e. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:312, 313, and 314, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:315, 316, and 317, respectively; f. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:318, 319, and 320, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:321, 322, and 323, respectively; g. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:324, 325, and 326, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:327, 328, and 329, respectively; h. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:330, 331, and 332, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:333, 334, and 335, respectively; i. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:336, 337, and 338, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:339, 340, and 341, respectively; j. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:342, 343, and 344, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:345, 346, and 347, respectively; k. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:348, 349, and 350, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:351, 352, and 353, respectively; l. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:354, 355, and 356, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:357, 358, and 359, respectively; m. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:360, 361, and 362, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:363, 364, and 365, respectively; n. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:366, 367, and 368, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:369, 370, and 371, respectively; o. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:372, 373, and 374, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:375, 376, and 377, respectively; p. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:378, 379, and 380, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:381, 382, and 383, respectively; q. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:384, 385, and 386, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:387, 388, and 389, respectively; r. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:390, 391, and 392, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:393, 394, and 395, respectively; s. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:396, 397, and 398, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:399, 400, and 401, respectively; t. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:402, 403, and 404, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:405, 406, and 407, respectively; u. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:408, 409, and 410, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:411, 412, and 413, respectively; v. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:420, 421, and 422, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:423, 424, and 425, respectively; w. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:426, 427, and 428, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:429, 430, and 431, respectively; x. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:432, 433, and 434, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:435, 436, and 437, respectively; y. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:438, 439, and 440, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:441, 442, and 443, respectively; z. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:444, 445, and 446, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:447, 448, and 449, respectively; aa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:450, 451, and 452, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:453, 454, and 455, respectively; bb. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:456, 457, and 458, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:459, 460, and 461, respectively; cc. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:462, 463, and 464, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:465, 466, and 467, respectively; dd. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:468, 469, and 470, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:471, 472, and 473, respectively; ee. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:474, 475, and 476, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:477, 478, and 479, respectively; ff. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:480, 481, and 482, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:483, 484, and 485, respectively; gg. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:486, 487, and 488, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:489, 490, and 491, respectively; hh. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:492, 493, and 494, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:495, 496, and 497, respectively; ii. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:498, 499, and 500, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:501, 502, and 503, respectively; jj. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:504, 505, and 506, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:507, 508, and 509, respectively; kk. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:510, 511, and 512, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:513, 514, and 515, respectively; ll. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:516, 517, and 518, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:519, 520, and 521, respectively; mm. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:522, 523, and 524, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:525, 526, and 527, respectively; nn. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:528, 529, and 530, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:531, 532, and 533, respectively; oo. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:540, 541, and 542, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:543, 544, and 545, respectively; pp. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:546, 547, and 548, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:549, 550, and 551, respectively; qq. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:552, 553, and 554, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:555, 556, and 557, respectively; rr. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:558, 559, and 560, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:561, 562, and 563, respectively; ss. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:564, 565, and 566, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:567, 568, and 569, respectively; tt. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:570, 571, and 572, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:573, 574, and 575, respectively; uu. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:576, 577, and 578, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:579, 580, and 581, respectively; vv. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:582, 583, and 584, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:585, 586, and 587, respectively; ww. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:600, 601, and 602, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:603, 604, and 605, respectively; xx. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:606, 607, and 608, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:609, 610, and 611, respectively; yy. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:612, 613, and 614, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:615, 616, and 617, respectively; zz. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:618, 619, and 620, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:621, 622, and 623, respectively; aaa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:624, 625, and 626, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:627, 628, and 629, respectively; bbb. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:630, 631, and 632, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:633, 634, and 635, respectively; ccc. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:636, 637, and 638, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:639, 640, and 641, respectively; ddd. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:642, 643, and 644, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:645, 646, and 647, respectively; eee. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:648, 649, and 650, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:651, 652, and 653, respectively; fff. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:654, 655, and 656, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:657, 658, and 659, respectively; ggg. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:666, 667, and 668, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:669, 670, and 671, respectively; hhh. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:900, 901, and 902, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:903, 904, and 905, respectively; iii. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:906, 907, and 908, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:909, 910, and 911, respectively; jjj. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:912, 913, and 914, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:915, 916, and 917, respectively; kkk. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:918, 919, and 920, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:921, 922, and 923, respectively; lll. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:936, 937, and 938, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; mmm. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:960, 961, and 962, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:963, 964, and 965, respectively; nnn. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:966, 967, and 968, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:969, 970, and 971, respectively; ooo. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:972, 973, and 974, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:975, 976, and 977, respectively; ppp. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:978, 979, and 980, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:981, 982, and 983, respectively; qqq. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:984, 985, and 986, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:987, 988, and 989, respectively; rrr. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:990, 991, and 992, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:993, 994, and 995, respectively; sss. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:996, 997, and 998, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:999, 1000, and 1001, respectively; ttt. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1002, 1003, and 1004, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1005, 1006, and 1007, respectively; uuu. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1008, 1009, and 1010, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1011, 1012, and 1013, respectively; vvv. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1014, 1015, and 1016, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1017, 1018, and 1019, respectively; www. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1020, 1021, and 1022, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1023, 1024, and 1025, respectively; xxx. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1026, 1027, and 1028, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1029, 1030, and 1031, respectively; yyy. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1032, 1033, and 1034, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1035, 1036, and 1037, respectively; zzz. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1038, 1039, and 1040, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1041, 1042, and 1043, respectively; aaaa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1050, 1051, and 1052, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1053, 1054, and 1055, respectively; bbbb. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1056, 1057, and 1058, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1059, 1060, and 1061, respectively; cccc. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1062, 1063, and 1064, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1065, 1066, and 1067, respectively; dddd. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1068, 1069, and 1070, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1071, 1072, and 1073, respectively; eeee. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1080, 1081, and 1082, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1083, 1084, and 1085, respectively; ffff. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1086, 1087, and 1088, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1089, 1090, and 1091, respectively; gggg. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1092, 1093, and 1094, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1095, 1096, and 1097, respectively; hhhh. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1098, 1099, and 1100, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1101, 1102, and 1103, respectively; iiii. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1104, 1105, and 1106, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1107, 1108, and 1109, respectively; jjjj. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1110, 1111, and 1112, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1113, 1114, and 1115, respectively; kkkk. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1116, 1117, and 1118, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1119, 1120, and 1121, respectively; llll. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1122, 1123, and 1124, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1125, 1126, and 1127, respectively; mmmm. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1128, 1129, and 1130, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1131, 1132, and 1133, respectively; nnnn. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1134, 1135, and 1136, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1137, 1138, and 1139, respectively; oooo. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1140, 1141, and 1142, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1143, 1144, and 1145, respectively; pppp. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1146, 1147, and 1148, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1149, 1150, and 1151, respectively; qqqq. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1152, 1153, and 1154, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1155, 1156, and 1157, respectively; rrrr. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1158, 1159, and 1160, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1161, 1162, and 1163, respectively; ssss. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1164, 1165, and 1166, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1167, 1168, and 1169, respectively; tttt. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1170, 1171, and 1172, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1173, 1174, and 1175, respectively; uuuu. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1176, 1177, and 1178, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1179, 1180, and 1181, respectively; vvvv. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1182, 1183, and 1184, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1185, 1186, and 1187, respectively; wwww. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1188, 1189, and 1190, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1191, 1192, and 1193, respectively; xxxx. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1194, 1195, and 1196, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1197, 1198, and 1199, respectively; yyyy. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1200, 1201, and 1202, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1203, 1204, and 1205, respectively; zzzz. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1206, 1207, and 1208, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1209, 1210, and 1211, respectively; or aaaaa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1212, 1213, and 1214, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1215, 1216, and 1217, respectively. 21. The isolated monoclonal antibody or antigen binding fragment thereof of claim 20 comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:138, and a VL comprising the amino acid sequence of SEQ ID NO:139; b. a VH comprising the amino acid sequence of SEQ ID NO:142, and a VL comprising the amino acid sequence of SEQ ID NO:143; c. a VH comprising the amino acid sequence of SEQ ID NO:144, and a VL comprising the amino acid sequence of SEQ ID NO:145; d. a VH comprising the amino acid sequence of SEQ ID NO:148, and a VL comprising the amino acid sequence of SEQ ID NO:149; e. a VH comprising the amino acid sequence of SEQ ID NO:150, and a VL comprising the amino acid sequence of SEQ ID NO:151; f. a VH comprising the amino acid sequence of SEQ ID NO:152, and a VL comprising the amino acid sequence of SEQ ID NO:153; g. a VH comprising the amino acid sequence of SEQ ID NO:154, and a VL comprising the amino acid sequence of SEQ ID NO:155; h. a VH comprising the amino acid sequence of SEQ ID NO:156, and a VL comprising the amino acid sequence of SEQ ID NO:157; i. a VH comprising the amino acid sequence of SEQ ID NO:158, and a VL comprising the amino acid sequence of SEQ ID NO:159; j. a VH comprising the amino acid sequence of SEQ ID NO:160, and a VL comprising the amino acid sequence of SEQ ID NO:161; k. a VH comprising the amino acid sequence of SEQ ID NO:162, and a VL comprising the amino acid sequence of SEQ ID NO:163; l. a VH comprising the amino acid sequence of SEQ ID NO:164, and a VL comprising the amino acid sequence of SEQ ID NO:165; m. a VH comprising the amino acid sequence of SEQ ID NO:166, and a VL comprising the amino acid sequence of SEQ ID NO:167; n. a VH comprising the amino acid sequence of SEQ ID NO:168, and a VL comprising the amino acid sequence of SEQ ID NO:169; o. a VH comprising the amino acid sequence of SEQ ID NO:170, and a VL comprising the amino acid sequence of SEQ ID NO:171; p. a VH comprising the amino acid sequence of SEQ ID NO:172, and a VL comprising the amino acid sequence of SEQ ID NO:173; q. a VH comprising the amino acid sequence of SEQ ID NO:174, and a VL comprising the amino acid sequence of SEQ ID NO:175; r. a VH comprising the amino acid sequence of SEQ ID NO:176, and a VL comprising the amino acid sequence of SEQ ID NO:177; s. a VH comprising the amino acid sequence of SEQ ID NO:178, and a VL comprising the amino acid sequence of SEQ ID NO:179; t. a VH comprising the amino acid sequence of SEQ ID NO:180, and a VL comprising the amino acid sequence of SEQ ID NO:181; u. a VH comprising the amino acid sequence of SEQ ID NO:182, and a VL comprising the amino acid sequence of SEQ ID NO:183; v. a VH comprising the amino acid sequence of SEQ ID NO:186, and a VL comprising the amino acid sequence of SEQ ID NO:187; w. a VH comprising the amino acid sequence of SEQ ID NO:188, and a VL comprising the amino acid sequence of SEQ ID NO:189; x. a VH comprising the amino acid sequence of SEQ ID NO:190, and a VL comprising the amino acid sequence of SEQ ID NO:191; y. a VH comprising the amino acid sequence of SEQ ID NO:192, and a VL comprising the amino acid sequence of SEQ ID NO:193; z. a VH comprising the amino acid sequence of SEQ ID NO:194, and a VL comprising the amino acid sequence of SEQ ID NO:195; aa. a VH comprising the amino acid sequence of SEQ ID NO:196, and a VL comprising the amino acid sequence of SEQ ID NO:197; bb. a VH comprising the amino acid sequence of SEQ ID NO:198, and a VL comprising the amino acid sequence of SEQ ID NO:199; cc. a VH comprising the amino acid sequence of SEQ ID NO:200, and a VL comprising the amino acid sequence of SEQ ID NO:201; dd. a VH comprising the amino acid sequence of SEQ ID NO:202, and a VL comprising the amino acid sequence of SEQ ID NO:203; ee. a VH comprising the amino acid sequence of SEQ ID NO:204, and a VL comprising the amino acid sequence of SEQ ID NO:205; ff. a VH comprising the amino acid sequence of SEQ ID NO:206, and a VL comprising the amino acid sequence of SEQ ID NO:207; gg. a VH comprising the amino acid sequence of SEQ ID NO:208, and a VL comprising the amino acid sequence of SEQ ID NO:209; hh. a VH comprising the amino acid sequence of SEQ ID NO:210, and a VL comprising the amino acid sequence of SEQ ID NO:211; ii. a VH comprising the amino acid sequence of SEQ ID NO:212, and a VL comprising the amino acid sequence of SEQ ID NO:213; jj. a VH comprising the amino acid sequence of SEQ ID NO:214, and a VL comprising the amino acid sequence of SEQ ID NO:215; kk. a VH comprising the amino acid sequence of SEQ ID NO:216, and a VL comprising the amino acid sequence of SEQ ID NO:217; ll. a VH comprising the amino acid sequence of SEQ ID NO:218, and a VL comprising the amino acid sequence of SEQ ID NO:219; mm. a VH comprising the amino acid sequence of SEQ ID NO:220, and a VL comprising the amino acid sequence of SEQ ID NO:221; nn. a VH comprising the amino acid sequence of SEQ ID NO:222, and a VL comprising the amino acid sequence of SEQ ID NO:223; oo. a VH comprising the amino acid sequence of SEQ ID NO:226, and a VL comprising the amino acid sequence of SEQ ID NO:227; pp. a VH comprising the amino acid sequence of SEQ ID NO:228, and a VL comprising the amino acid sequence of SEQ ID NO:229; qq. a VH comprising the amino acid sequence of SEQ ID NO:230, and a VL comprising the amino acid sequence of SEQ ID NO:231; rr. a VH comprising the amino acid sequence of SEQ ID NO:232, and a VL comprising the amino acid sequence of SEQ ID NO:233; ss. a VH comprising the amino acid sequence of SEQ ID NO:234, and a VL comprising the amino acid sequence of SEQ ID NO:235; tt. a VH comprising the amino acid sequence of SEQ ID NO:236, and a VL comprising the amino acid sequence of SEQ ID NO:237; uu. a VH comprising the amino acid sequence of SEQ ID NO:238, and a VL comprising the amino acid sequence of SEQ ID NO:239; vv. a VH comprising the amino acid sequence of SEQ ID NO:240, and a VL comprising the amino acid sequence of SEQ ID NO:241; ww. a VH comprising the amino acid sequence of SEQ ID NO:246, and a VL comprising the amino acid sequence of SEQ ID NO:247; xx. a VH comprising the amino acid sequence of SEQ ID NO:248, and a VL comprising the amino acid sequence of SEQ ID NO:249; yy. a VH comprising the amino acid sequence of SEQ ID NO:250, and a VL comprising the amino acid sequence of SEQ ID NO:251; zz. a VH comprising the amino acid sequence of SEQ ID NO:252, and a VL comprising the amino acid sequence of SEQ ID NO:253; aaa. a VH comprising the amino acid sequence of SEQ ID NO:254, and a VL comprising the amino acid sequence of SEQ ID NO:255; bbb. a VH comprising the amino acid sequence of SEQ ID NO:256, and a VL comprising the amino acid sequence of SEQ ID NO:257; ccc. a VH comprising the amino acid sequence of SEQ ID NO:258, and a VL comprising the amino acid sequence of SEQ ID NO:259; ddd. a VH comprising the amino acid sequence of SEQ ID NO:260, and a VL comprising the amino acid sequence of SEQ ID NO:261; eee. a VH comprising the amino acid sequence of SEQ ID NO:262, and a VL comprising the amino acid sequence of SEQ ID NO:263; fff. a VH comprising the amino acid sequence of SEQ ID NO:264, and a VL comprising the amino acid sequence of SEQ ID NO:265; ggg. a VH comprising the amino acid sequence of SEQ ID NO:268, and a VL comprising the amino acid sequence of SEQ ID NO:269; hhh. a VH comprising the amino acid sequence of SEQ ID NO:786, and a VL comprising the amino acid sequence of SEQ ID NO:787; iii. a VH comprising the amino acid sequence of SEQ ID NO:788, and a VL comprising the amino acid sequence of SEQ ID NO:789; jjj. a VH comprising the amino acid sequence of SEQ ID NO:790, and a VL comprising the amino acid sequence of SEQ ID NO:791; kkk. a VH comprising the amino acid sequence of SEQ ID NO:792, and a VL comprising the amino acid sequence of SEQ ID NO:793; lll. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; mmm. a VH comprising the amino acid sequence of SEQ ID NO:806, and a VL comprising the amino acid sequence of SEQ ID NO:807; nnn. a VH comprising the amino acid sequence of SEQ ID NO:808, and a VL comprising the amino acid sequence of SEQ ID NO:809; ooo. a VH comprising the amino acid sequence of SEQ ID NO:810, and a VL comprising the amino acid sequence of SEQ ID NO:811; ppp. a VH comprising the amino acid sequence of SEQ ID NO:812, and a VL comprising the amino acid sequence of SEQ ID NO:813; qqq. a VH comprising the amino acid sequence of SEQ ID NO:814, and a VL comprising the amino acid sequence of SEQ ID NO:815; rrr. a VH comprising the amino acid sequence of SEQ ID NO:816, and a VL comprising the amino acid sequence of SEQ ID NO:817; sss. a VH comprising the amino acid sequence of SEQ ID NO:818, and a VL comprising the amino acid sequence of SEQ ID NO:819; ttt. a VH comprising the amino acid sequence of SEQ ID NO:820, and a VL comprising the amino acid sequence of SEQ ID NO:821; uuu. a VH comprising the amino acid sequence of SEQ ID NO:822, and a VL comprising the amino acid sequence of SEQ ID NO:823; vvv. a VH comprising the amino acid sequence of SEQ ID NO:824, and a VL comprising the amino acid sequence of SEQ ID NO:825; www. a VH comprising the amino acid sequence of SEQ ID NO:826, and a VL comprising the amino acid sequence of SEQ ID NO:827; xxx. a VH comprising the amino acid sequence of SEQ ID NO:828, and a VL comprising the amino acid sequence of SEQ ID NO:829; yyy. a VH comprising the amino acid sequence of SEQ ID NO:830, and a VL comprising the amino acid sequence of SEQ ID NO:831; zzz. a VH comprising the amino acid sequence of SEQ ID NO:832, and a VL comprising the amino acid sequence of SEQ ID NO:833; aaaa. a VH comprising the amino acid sequence of SEQ ID NO:836, and a VL comprising the amino acid sequence of SEQ ID NO:837; bbbb. a VH comprising the amino acid sequence of SEQ ID NO:838, and a VL comprising the amino acid sequence of SEQ ID NO:839; cccc. a VH comprising the amino acid sequence of SEQ ID NO:840, and a VL comprising the amino acid sequence of SEQ ID NO:841; dddd. a VH comprising the amino acid sequence of SEQ ID NO: 842, and a VL comprising the amino acid sequence of SEQ ID NO:843; eeee. a VH comprising the amino acid sequence of SEQ ID NO:846, and a VL comprising the amino acid sequence of SEQ ID NO:847; ffff. a VH comprising the amino acid sequence of SEQ ID NO:848, and a VL comprising the amino acid sequence of SEQ ID NO:849; gggg. a VH comprising the amino acid sequence of SEQ ID NO:850, and a VL comprising the amino acid sequence of SEQ ID NO:851; hhhh. a VH comprising the amino acid sequence of SEQ ID NO:852, and a VL comprising the amino acid sequence of SEQ ID NO:853; iiii. a VH comprising the amino acid sequence of SEQ ID NO:854, and a VL comprising the amino acid sequence of SEQ ID NO:855; jjjj. a VH comprising the amino acid sequence of SEQ ID NO:856, and a VL comprising the amino acid sequence of SEQ ID NO:857; kkkk. a VH comprising the amino acid sequence of SEQ ID NO:858, and a VL comprising the amino acid sequence of SEQ ID NO:859; llll. a VH comprising the amino acid sequence of SEQ ID NO:860, and a VL comprising the amino acid sequence of SEQ ID NO:861; mmmm. a VH comprising the amino acid sequence of SEQ ID NO:862, and a VL comprising the amino acid sequence of SEQ ID NO:863; nnnn. a VH comprising the amino acid sequence of SEQ ID NO:864, and a VL comprising the amino acid sequence of SEQ ID NO:865; oooo. a VH comprising the amino acid sequence of SEQ ID NO:866, and a VL comprising the amino acid sequence of SEQ ID NO:867; pppp. a VH comprising the amino acid sequence of SEQ ID NO:868, and a VL comprising the amino acid sequence of SEQ ID NO:869; qqqq. a VH comprising the amino acid sequence of SEQ ID NO:870, and a VL comprising the amino acid sequence of SEQ ID NO:871; rrrr. a VH comprising the amino acid sequence of SEQ ID NO:872, and a VL comprising the amino acid sequence of SEQ ID NO:873; ssss. a VH comprising the amino acid sequence of SEQ ID NO:874, and a VL comprising the amino acid sequence of SEQ ID NO:875; tttt. a VH comprising the amino acid sequence of SEQ ID NO:876, and a VL comprising the amino acid sequence of SEQ ID NO:877; uuuu. a VH comprising the amino acid sequence of SEQ ID NO:878, and a VL comprising the amino acid sequence of SEQ ID NO:879; vvvv. a VH comprising the amino acid sequence of SEQ ID NO:880, and a VL comprising the amino acid sequence of SEQ ID NO:881; wwww. a VH comprising the amino acid sequence of SEQ ID NO:882, and a VL comprising the amino acid sequence of SEQ ID NO:883; xxxx. a VH comprising the amino acid sequence of SEQ ID NO:884, and a VL comprising the amino acid sequence of SEQ ID NO:885; yyyy. a VH comprising the amino acid sequence of SEQ ID NO:886, and a VL comprising the amino acid sequence of SEQ ID NO:887; zzzz. a VH comprising the amino acid sequence of SEQ ID NO:888, and a VL comprising the amino acid sequence of SEQ ID NO:889; or aaaaa. a VH comprising the amino acid sequence of SEQ ID NO:890, and a VL comprising the amino acid sequence of SEQ ID NO:891. 22. The antibody or fragment of any one of claims 1-21, wherein the antibody is an IgG. 23. The antibody or fragment of any one of claims 1-22, wherein the antibody is a humanized or chimeric antibody or fragment thereof. 24. The isolated antibody or fragment of any one of claims 1-22 which is an antibody or fragment thereof wherein the isolated antibody is a form of an antibody F(ab')2, scFv fragment, domain antibody, minibody, diabody, triabody or tetrabody. 25. The antibody of any one of claims 1-24, wherein the antibody is genetically fused or chemically conjugated to an agent; wherein: optionally the agent is a detectable substance or is a drug, wherein: optionally the detectable substance is selected from enzymes, prosthetic groups, fluorescent materials, luminescent materials, bioluminescent materials or chemiluminescent materials, wherein: optionally the enzymes are selected from horseradish peroxidase, alkaline phosphatase, beta-galactosidase, or acetylcholinesterase; optionally the prosthetic groups are selected from streptavidin/biotin or avidin/biotin; optionally the fluorescent materials are selected from umbelliferone, fluorescein, fluorescein isothiocynate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride, or phycoerythrin; optionally the chemiluminescent materials are selected from 225Acγ-emitting, Auger- emitting, β-emitting, an alpha-emitting or positron-emitting radioactive isotope; optionally the luminescent material is luminol; and wherein: optionally the bioluminescent materials are selected from luciferase, luciferin, or aequorin. 26. A nucleic acid molecule encoding the antibody of any one of claims 1-24. 27. A vector comprising the nucleic acid molecule of claim 26. 28. A host cell transformed with the vector of claim 27. 29. A composition comprising the antibody of any one of claims 1-25, the nucleic acid molecule of claim 26, or the vector of claim 27, and a pharmaceutically acceptable excipient. 30. A kit comprising the antibody of any one of claims 1-25. 31. A method for detecting, selecting and/or enriching Interleukin-23 receptor (IL-23R) in a sample comprising contacting the sample with the antibody of any one of claims 1 to 25, wherein: optionally the method comprises using the antibody of any one of claims 1 to 25 in an immunohistochemistry (IHC) assay, an immunocytochemistry (ICC) assay, an immunoblotting assay, an immunoprecipitation assay, a flow cytometry assay, an ELISA, a radioimmunoassay, a mass spectrometry assay, or high throughput screening assay; wherein: optionally the flow cytometry assay comprises three-steps of staining: (1) first, incubating the sample with the antibody of any one of claims 1 to 25; (2) second, incubating the sample with biotinylated anti-mouse IgG2a; (3) third, incubating the sample with streptavidin-PE; and wherein: optionally, to establish background for the flow cytometry assay, cells are incubated with buffer alone or the negative control antibody are used as a control group in step (1), and cells are incubated without the biotinylated anti-mouse IgG2a secondary reagent are used as an additional control group in step (2). 32. A method for detecting, selecting and/or enriching interleukin-23 receptor (IL-23R) in a sample comprising contacting the sample with an antibody that binds to a same epitope as the antibody of any one of claims 1 to 25, or an antibody that binds IL-23R competitively with the antibody of any one of claims 1 to 25. 33. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:202 and a VL comprising the amino acid sequence of SEQ ID NO:203; b. a VH comprising the amino acid sequence of SEQ ID NO:252 and a VL comprising the amino acid sequence of SEQ ID NO:253; or c. a VH comprising the amino acid sequence of SEQ ID NO:156 and a VL comprising the amino acid sequence of SEQ ID NO:157. 34. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:192 and a VL comprising the amino acid sequence of SEQ ID NO:193; b. a VH comprising the amino acid sequence of SEQ ID NO:194 and a VL comprising the amino acid sequence of SEQ ID NO:195; c. a VH comprising the amino acid sequence of SEQ ID NO:200 and a VL comprising the amino acid sequence of SEQ ID NO:201; d. a VH comprising the amino acid sequence of SEQ ID NO:218 and a VL comprising the amino acid sequence of SEQ ID NO:219; e. a VH comprising the amino acid sequence of SEQ ID NO:222 and a VL comprising the amino acid sequence of SEQ ID NO:223; f. a VH comprising the amino acid sequence of SEQ ID NO:260 and a VL comprising the amino acid sequence of SEQ ID NO:261; g. a VH comprising the amino acid sequence of SEQ ID NO:264 and a VL comprising the amino acid sequence of SEQ ID NO:265; h. a VH comprising the amino acid sequence of SEQ ID NO:154 and a VL comprising the amino acid sequence of SEQ ID NO:155; i. a VH comprising the amino acid sequence of SEQ ID NO:160 and a VL comprising the amino acid sequence of SEQ ID NO:161; or j. a VH comprising the amino acid sequence of SEQ ID NO:164 and a VL comprising the amino acid sequence of SEQ ID NO:165. 35. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:786 and a VL comprising the amino acid sequence of SEQ ID NO:787; b. a VH comprising the amino acid sequence of SEQ ID NO:790 and a VL comprising the amino acid sequence of SEQ ID NO:791; c. a VH comprising the amino acid sequence of SEQ ID NO:792 and a VL comprising the amino acid sequence of SEQ ID NO:793; d. a VH comprising the amino acid sequence of SEQ ID NO:236 and a VL comprising the amino acid sequence of SEQ ID NO:237; e. a VH comprising the amino acid sequence of SEQ ID NO:826 and a VL comprising the amino acid sequence of SEQ ID NO:827; or f. a VH comprising the amino acid sequence of SEQ ID NO:828 and a VL comprising the amino acid sequence of SEQ ID NO:829. 36. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:196 and a VL comprising the amino acid sequence of SEQ ID NO:197; b. a VH comprising the amino acid sequence of SEQ ID NO:262 and a VL comprising the amino acid sequence of SEQ ID NO:263; or c. a VH comprising the amino acid sequence of SEQ ID NO:152 and a VL comprising the amino acid sequence of SEQ ID NO:153. 37. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:798 and a VL comprising the amino acid sequence of SEQ ID NO:799. 38. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:206 and a VL comprising the amino acid sequence of SEQ ID NO:207; b. a VH comprising the amino acid sequence of SEQ ID NO:250 and a VL comprising the amino acid sequence of SEQ ID NO:251; c. a VH comprising the amino acid sequence of SEQ ID NO:144 and a VL comprising the amino acid sequence of SEQ ID NO:145; or d. a VH comprising the amino acid sequence of SEQ ID NO:170 and a VL comprising the amino acid sequence of SEQ ID NO:171. 39. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: e. a VH comprising the amino acid sequence of SEQ ID NO:150 and a VL comprising the amino acid sequence of SEQ ID NO:151. 40. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:198 and a VL comprising the amino acid sequence of SEQ ID NO:199; or b. a VH comprising the amino acid sequence of SEQ ID NO:240 and a VL comprising the amino acid sequence of SEQ ID NO:241. 41. The method of claim 32, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:204 and a VL comprising the amino acid sequence of SEQ ID NO:205; or b. a VH comprising the amino acid sequence of SEQ ID NO:884 and a VL comprising the amino acid sequence of SEQ ID NO:885. 42. The method of any one of claims 31 to 41, wherein the method is for detecting, selecting and/or enriching human IL-23R, for detecting, selecting and/or enriching cells that express IL-23R, or for detecting denatured IL-23R. 43. The method of any one of claims 31 to 42, wherein: the method comprising contacting the sample with two or more antibodies each being the antibody of any one of claims 1 to 25, wherein: optionally the two or more antibodies bind to different epitopes of IL-23R. 44. The method of any one of claims 31 to 43, wherein the sample is from a human subject and wherein the human subject has a disease or disorder which is an IL-23R associated disease or disorder. 45. A method of treating a disease or disorder in a subject, comprising administering to the subject the composition of claim 29, wherein the disease or disorder is an IL-23R associated disease or disorder. 46. The method according to claim 45, wherein the disease or disorder is selected from multiple sclerosis, asthma, rheumatoid arthritis, inflammation of the gut, inflammatory bowel diseases (IBDs), juvenile IBD, adolescent IBD, Crohn’s disease, ulcerative colitis, Celiac disease (nontropical Sprue), microscopic colitis, collagenous colitis, eosinophilic gastroenteritis/esophagitis, colitis associated with radio- or chemo-therapy, colitis associated with disorders of innate immunity as in leukocyte adhesion deficiency-1, sarcoidosis, Systemic Lupus Erythematosus, ankylosing spondylitis (axial spondyloarthritis), psoriatic arthritis, psoriasis (e.g., plaque psoriasis, guttate psoriasis, inverse psoriasis, pustular psoriasis, Palmo-Plantar Pustulosis, psoriasis vulgaris, or erythrodermic psoriasis), atopic dermatitis, acne ectopica, enteropathy associated with seronegative arthropathies, chronic granulomatous disease, glycogen storage disease type 1b, Hermansky-Pudlak syndrome, Chediak- Higashi syndrome, Wiskott-Aldrich Syndrome, pouchitis, pouchitis resulting after proctocolectomy and ileoanal anastomosis, gastrointestinal cancer, pancreatitis, insulin-dependent diabetes mellitus, mastitis, cholecystitis, cholangitis, primary biliary cirrhosis, viral-associated enteropathy, pericholangitis, chronic bronchitis, chronic sinusitis, asthma, uveitis, or graft versus host disease. 47. Use of: an antibody or antigen binding fragment thereof of any of claims 1-25; or a composition of claim 29 in manufacture of a medicament for treatment of an IL-23R associated disease or disorder; and wherein the disease or disorder is associated with inflammatory, autoimmune inflammation diseases and/or related disorders. 48. The antibody or antigen binding fragment of any of claims 1-25 or the composition of claim 29 for use in the treatment of an IL-23R associated disease or disorder; wherein the disease or disorder is associated with inflammatory, autoimmune inflammation diseases and/or related disorders |
[00202] Amino acids may be grouped according to similarities in the properties of their side chains (see, e.g., Lehninger, Biochemistry 73-75 (2d ed.1975)): (1) non-polar: Ala (A), Val (V), Leu (L), Ile (I), Pro (P), Phe (F), Trp (W), Met (M); (2) uncharged polar: Gly (G), Ser (S), Thr (T), Cys (C), Tyr (Y), Asn (N), Gln (Q); (3) acidic: Asp (D), Glu (E); and (4) basic: Lys (K), Arg (R), His(H). Alternatively, naturally occurring residues may be divided into groups based on common side-chain properties: (1) hydrophobic: Norleucine, Met, Ala, Val, Leu, Ile; (2) neutral hydrophilic: Cys, Ser, Thr, Asn, Gln; (3) acidic: Asp, Glu; (4) basic: His, Lys, Arg; (5) residues that influence chain orientation: Gly, Pro; and (6) aromatic: Trp, Tyr, Phe. For example, any cysteine residue not involved in maintaining the proper conformation of the antibody also may be substituted, for example, with another amino acid, such as alanine or serine, to improve the oxidative stability of the molecule and to prevent aberrant crosslinking. Non-conservative substitutions will entail exchanging a member of one of these classes for another class. [00203] One type of substitutional variant involves substituting one or more hypervariable region residues of a parent antibody (e.g., a humanized or human antibody). Generally, the resulting variant(s) selected for further study will have modifications (e.g., improvements) in certain biological properties (e.g., increased affinity, reduced immunogenicity) relative to the parent antibody and/or will have substantially retained certain biological properties of the parent antibody. An exemplary substitutional variant is an affinity matured antibody, which may be conveniently generated, e.g., using phage display-based affinity maturation techniques such as those described herein. Briefly, one or more CDR residues are mutated and the variant antibodies displayed on phage and screened for a particular biological activity (e.g. binding affinity). [00204] Alterations (e.g., substitutions) may be made in CDRs, e.g., to improve antibody affinity. Such alterations may be made in CDR “hotspots,” i.e., residues encoded by codons that undergo mutation at high frequency during the somatic maturation process (see, e.g., Chowdhury, Methods Mol. Biol.207:179-196 (2008)), and/or SDRs (a-CDRs), with the resulting variant antibody or fragment thereof being tested for binding affinity. Affinity maturation by constructing and reselecting from secondary libraries has been described, e.g., in Hoogenboom et al. in Methods in Molecular Biology 178:1-37 (O’Brien et al., ed., Human Press, Totowa, NJ, (2001).) In some embodiments of affinity maturation, diversity is introduced into the variable genes chosen for maturation by any of a variety of methods (e.g., error-prone PCR, chain shuffling, or oligonucleotide- directed mutagenesis). A secondary library is then created. The library is then screened to identify any antibody variants with the desired affinity. Another method to introduce diversity involves CDR- directed approaches, in which several CDR residues (e.g., 4-6 residues at a time) are randomized. CDR residues involved in antigen binding may be specifically identified, e.g., using alanine scanning mutagenesis or modeling. More detailed description regarding affinity maturation is provided in the section below. [00205] In some embodiments, substitutions, insertions, or deletions may occur within one or more CDRs so long as such alterations do not substantially reduce the ability of the antibody to bind antigen. For example, conservative alterations (e.g., conservative substitutions as provided herein) that do not substantially reduce binding affinity may be made in CDRs. In some embodiments of the variant antibody sequences provided herein, each CDR either is unaltered, or contains no more than one, two or three amino acid substitutions. [00206] A useful method for identification of residues or regions of an antibody that may be targeted for mutagenesis is called “alanine scanning mutagenesis” as described by Cunningham and Wells, Science, 244:1081-1085 (1989). In this method, a residue or group of target residues (e.g., charged residues such as Arg, Asp, His, Lys, and Glu) are identified and replaced by a neutral or negatively charged amino acid (e.g., alanine or polyalanine) to determine whether the interaction of the antibody with antigen is affected. Further substitutions may be introduced at the amino acid locations demonstrating functional sensitivity to the initial substitutions. Alternatively, or additionally, a crystal structure of an antigen-antibody complex to identify contact points between the antibody and antigen. Such contact residues and neighboring residues may be targeted or eliminated as candidates for substitution. Variants may be screened to determine whether they contain the desired properties. [00207] Amino acid sequence insertions include amino- and/or carboxyl-terminal fusions ranging in length from one residue to polypeptides containing a hundred or more residues, as well as intrasequence insertions of single or multiple amino acid residues. Examples of terminal insertions include an antibody with an N-terminal methionyl residue. Other insertional variants of the antibody molecule include the fusion to the N- or C-terminus of the antibody to an enzyme (e.g., for ADEPT) or a polypeptide which increases the serum half-life of the antibody. [00208] The variations can be made using methods known in the art such as oligonucleotide- mediated (site-directed) mutagenesis, alanine scanning, and PCR mutagenesis. Site-directed mutagenesis (see, e.g., Carter, Biochem J.237:1-7 (1986); and Zoller et al., Nucl. Acids Res. 10:6487-500 (1982)), cassette mutagenesis (see, e.g., Wells et al., Gene 34:315-23 (1985)), or other known techniques can be performed on the cloned DNA to produce the antibody variant DNA. In vitro Affinity Maturation [00209] In some embodiments, antibody variants having an improved property such as affinity, stability, or expression level as compared to a parent antibody may be prepared by in vitro affinity maturation. Like the natural prototype, in vitro affinity maturation is based on the principles of mutation and selection. Libraries of antibodies are displayed on the surface of an organism (e.g., phage, bacteria, yeast, or mammalian cell) or in association (e.g., covalently or non-covalently) with their encoding mRNA or DNA. Affinity selection of the displayed antibodies allows isolation of organisms or complexes carrying the genetic information encoding the antibodies. Two or three rounds of mutation and selection using display methods such as phage display usually results in antibody fragments with affinities in the low nanomolar range. Affinity matured antibodies can have nanomolar or even picomolar affinities for the target antigen. [00210] Phage display is a widespread method for display and selection of antibodies. The antibodies are displayed on the surface of Fd or M13 bacteriophages as fusions to the bacteriophage coat protein. Selection involves exposure to antigen to allow phage-displayed antibodies to bind their targets, a process referred to as “panning.” Phage bound to antigen are recovered and used to infect bacteria to produce phage for further rounds of selection. For review, see, for example, Hoogenboom, Methods. Mol. Biol.178:1-37 (2002); and Bradbury and Marks, J. Immunol. Methods 290:29-49 (2004). [00211] In a yeast display system (see, e.g., Boder et al., Nat. Biotech.15:553–57 (1997); and Chao et al., Nat. Protocols 1:755-68 (2006)), the antibody may be fused to the adhesion subunit of the yeast agglutinin protein Aga2p, which attaches to the yeast cell wall through disulfide bonds to Aga1p. Display of a protein via Aga2p projects the protein away from the cell surface, minimizing potential interactions with other molecules on the yeast cell wall. Magnetic separation and flow cytometry are used to screen the library to select for antibodies with improved affinity or stability. Binding to a soluble antigen of interest is determined by labeling of yeast with biotinylated antigen and a secondary reagent such as streptavidin conjugated to a fluorophore. Variations in surface expression of the antibody can be measured through immunofluorescence labeling of either the hemagglutinin or c-Myc epitope tag flanking the single chain antibody (e.g., scFv). Expression has been shown to correlate with the stability of the displayed protein, and thus antibodies can be selected for improved stability as well as affinity (see, e.g., Shusta et al., J. Mol. Biol.292:949-56 (1999)). An additional advantage of yeast display is that displayed proteins are folded in the endoplasmic reticulum of the eukaryotic yeast cells, taking advantage of endoplasmic reticulum chaperones and quality-control machinery. Once maturation is complete, antibody affinity can be conveniently “titrated” while displayed on the surface of the yeast, eliminating the need for expression and purification of each clone. A theoretical limitation of yeast surface display is the potentially smaller functional library size than that of other display methods; however, a recent approach uses the yeast cells’ mating system to create combinatorial diversity estimated to be 10 14 in size (see, e.g., U.S. Pat. Publication 2003/0186374; and Blaise et al., Gene 342:211–18 (2004)). [00212] In ribosome display, antibody-ribosome-mRNA (ARM) complexes are generated for selection in a cell-free system. The DNA library coding for a particular library of antibodies is genetically fused to a spacer sequence lacking a stop codon. This spacer sequence, when translated, is still attached to the peptidyl tRNA and occupies the ribosomal tunnel, and thus allows the protein of interest to protrude out of the ribosome and fold. The resulting complex of mRNA, ribosome, and protein can bind to surface-bound ligand, allowing simultaneous isolation of the antibody and its encoding mRNA through affinity capture with the ligand. The ribosome-bound mRNA is then reverse transcribed back into cDNA, which can then undergo mutagenesis and be used in the next round of selection (see, e.g., Fukuda et al., Nucleic Acids Res.34:e127 (2006)). In mRNA display, a covalent bond between antibody and mRNA is established using puromycin as an adaptor molecule (Wilson et al., Proc. Natl. Acad. Sci. USA 98:3750-55 (2001)). [00213] As these methods are performed entirely in vitro, they provide two main advantages over other selection technologies. First, the diversity of the library is not limited by the transformation efficiency of bacterial cells, but only by the number of ribosomes and different mRNA molecules present in the test tube. Second, random mutations can be introduced easily after each selection round, for example, by non-proofreading polymerases, as no library must be transformed after any diversification step. [00214] In some embodiments, mammalian display systems may be used. [00215] Diversity may also be introduced into the CDRs of the antibody libraries in a targeted manner or via random introduction. The former approach includes sequentially targeting all the CDRs of an antibody via a high or low level of mutagenesis or targeting isolated hot spots of somatic hypermutations (see, e.g., Ho et al., J. Biol. Chem.280:607-17 (2005)) or residues suspected of affecting affinity on experimental basis or structural reasons. Diversity may also be introduced by replacement of regions that are naturally diverse via DNA shuffling or similar techniques (see, e.g., Lu et al., J. Biol. Chem.278:43496-507 (2003); U.S. Pat. Nos.5,565,332 and 6,989,250). Alternative techniques target hypervariable loops extending into framework-region residues (see, e.g., Bond et al., J. Mol. Biol.348:699-709 (2005)) employ loop deletions and insertions in CDRs or use hybridization- based diversification (see, e.g., U.S. Pat. Publication No.2004/0005709). Additional methods of generating diversity in CDRs are disclosed, for example, in U.S. Pat. No.7,985,840. Further methods that can be used to generate antibody libraries and/or antibody affinity maturation are disclosed, e.g., in U.S. Patent Nos.8,685,897 and 8,603,930, and U.S. Publ. Nos.2014/0170705, 2014/0094392, 2012/0028301, 2011/0183855, and 2009/0075378, each of which are incorporated herein by reference. [00216] Screening of the libraries can be accomplished by various techniques known in the art. For example, antibodies can be immobilized onto solid supports, columns, pins, or cellulose/poly (vinylidene fluoride) membranes/other filters, expressed on host cells affixed to adsorption plates or used in cell sorting, or conjugated to biotin for capture with streptavidin-coated beads or used in any other method for panning display libraries. [00217] For review of in vitro affinity maturation methods, see, e.g., Hoogenboom, Nature Biotechnology 23:1105-16 (2005); Quiroz and Sinclair, Revista Ingeneria Biomedia 4:39-51 (2010); and references therein. Modifications of Antibodies [00218] Covalent modifications of antibodies are included within the scope of the present disclosure. Covalent modifications include reacting targeted amino acid residues of an antibody with an organic derivatizing agent that is capable of reacting with selected side chains or the N- or C- terminal residues of the antibody. Other modifications include deamidation of glutaminyl and asparaginyl residues to the corresponding glutamyl and aspartyl residues, respectively, hydroxylation of proline and lysine, phosphorylation of hydroxyl groups of seryl or threonyl residues, methylation of the α-amino groups of lysine, arginine, and histidine side chains (see, e.g., Creighton, Proteins: Structure and Molecular Properties 79-86 (1983)), acetylation of the N-terminal amine, and amidation of any C-terminal carboxyl group. [00219] Other types of covalent modification of the antibody included within the scope of this present disclosure include altering the native glycosylation pattern of the antibody or polypeptide as described above (see, e.g., Beck et al., Curr. Pharm. Biotechnol.9:482-501 (2008); and Walsh, Drug Discov. Today 15:773-80 (2010)), and linking the antibody to one of a variety of nonproteinaceous polymers, e.g., polyethylene glycol (PEG), polypropylene glycol, or polyoxyalkylenes, in the manner set forth, for example, in U.S. Pat. Nos.4,640,835; 4,496,689; 4,301,144; 4,670,417; 4,791,192; or 4,179,337. The antibody that binds to IL-23R of the disclosure may also be genetically fused or conjugated to one or more immunoglobulin constant regions or portions thereof (e.g., Fc) to extend half-life and/or to impart known Fc-mediated effector functions. [00220] The antibody that binds to IL-23R of the present disclosure may also be modified to form chimeric molecules comprising the antibody that binds to IL-23R fused to another, heterologous polypeptide or amino acid sequence, for example, an epitope tag (see, e.g., Terpe, Appl. Microbiol. Biotechnol.60:523-33 (2003)) or the Fc region of an IgG molecule (see, e.g., Aruffo, Antibody Fusion Proteins 221-42 (Chamow and Ashkenazi eds., 1999)). [00221] Also provided herein are fusion proteins comprising the antibody that binds to IL- 23R of the disclosure and a heterologous polypeptide. In some embodiments, the heterologous polypeptide to which the antibody is genetically fused or chemically conjugated is useful for targeting the antibody to cells having cell surface-expressed IL-23R. [00222] Also provided herein are panels of antibodies that bind to an IL-23R antigen. In specific embodiments, the panels of antibodies have different association rates, different dissociation rates, different affinities for an IL-23R antigen, and/or different specificities for an IL-23R antigen. In some embodiments, the panels comprise or consist of about 10 to about 1000 antibodies or more. Panels of antibodies can be used, for example, in 96-well or 384-well plates, for assays such as ELISAs. Other Binding Molecules Comprising the Antibodies [00223] In another aspect, provided herein is a binding molecule comprising an anti-IL-23R antibody provided herein. In some embodiments, an antibody against IL-23R provided herein is part of other binding molecules. Exemplary binding molecules of the present disclosure are described herein. Fusion Protein [00224] In various embodiments, the antibody provided herein can be genetically fused or chemically conjugated to another agent, for example, protein-based entities. The antibody may be chemically-conjugated to the agent, or otherwise non-covalently conjugated to the agent. The agent can be a peptide or antibody (or a fragment thereof). [00225] Thus, in some embodiments, provided herein are antibodies that are recombinantly fused or chemically conjugated (covalent or non-covalent conjugations) to a heterologous protein or polypeptide (or fragment thereof, for example, to a polypeptide of about 10, about 20, about 30, about 40, about 50, about 60, about 70, about 80, about 90, about 100, about 150, about 200, about 250, about 300, about 350, about 400, about 450 or about 500 amino acids, or over 500 amino acids) to generate fusion proteins, as well as uses thereof. In particular, provided herein are fusion proteins comprising an antigen binding fragment of the antibody provided herein (e.g., CDR1, CDR2, and/or CDR3) and a heterologous protein, polypeptide, or peptide. [00226] Moreover, antibodies provided herein can be fused to marker or “tag” sequences, such as a peptide, to facilitate purification. In specific embodiments, the marker or tag amino acid sequence is a hexa-histidine peptide, hemagglutinin (“HA”) tag, and “FLAG” tag. [00227] Methods for fusing or conjugating moieties (including polypeptides) to antibodies are known (see, e.g., Arnon et al., Monoclonal Antibodies for Immunotargeting of Drugs in Cancer Therapy, in Monoclonal Antibodies and Cancer Therapy 243-56 (Reisfeld et al. eds., 1985); Hellstrom et al., Antibodies for Drug Delivery, in Controlled Drug Delivery 623-53 (Robinson et al. eds., 2d ed.1987); Thorpe, Antibody Carriers of Cytotoxic Agents in Cancer Therapy: A Review, in Monoclonal Antibodies: Biological and Clinical Applications 475-506 (Pinchera et al. eds., 1985); Analysis, Results, and Future Prospective of the Therapeutic Use of Radiolabeled Antibody in Cancer Therapy, in Monoclonal Antibodies for Cancer Detection and Therapy 303-16 (Baldwin et al. eds., 1985); Thorpe et al., Immunol. Rev.62:119-58 (1982); U.S. Pat. Nos.5,336,603; 5,622,929; 5,359,046; 5,349,053; 5,447,851; 5,723,125; 5,783,181; 5,908,626; 5,844,095; and 5,112,946; EP 307,434; EP 367,166; EP 394,827; PCT publications WO 91/06570, WO 96/04388, WO 96/22024, WO 97/34631, and WO 99/04813; Ashkenazi et al., Proc. Natl. Acad. Sci. USA, 88: 10535-39 (1991); Traunecker et al., Nature, 331:84-86 (1988); Zheng et al., J. Immunol.154:5590-600 (1995); and Vil et al., Proc. Natl. Acad. Sci. USA 89:11337-41 (1992)). [00228] Fusion proteins may be generated, for example, through the techniques of gene- shuffling, motif-shuffling, exon-shuffling, and/or codon-shuffling (collectively referred to as “DNA shuffling”). DNA shuffling may be employed to alter the activities of the antibodies as provided herein, including, for example, antibodies with higher affinities and lower dissociation rates (see, e.g., U.S. Pat. Nos.5,605,793; 5,811,238; 5,830,721; 5,834,252; and 5,837,458; Patten et al., Curr. Opinion Biotechnol.8:724-33 (1997); Harayama, Trends Biotechnol.16(2):76-82 (1998); Hansson et al., J. Mol. Biol.287:265-76 (1999); and Lorenzo and Blasco, Biotechniques 24(2):308-13 (1998)). Antibodies, or the encoded antibodies, may be altered by being subjected to random mutagenesis by error-prone PCR, random nucleotide insertion, or other methods prior to recombination. A polynucleotide encoding an antibody provided herein may be recombined with one or more components, motifs, sections, parts, domains, fragments, etc. of one or more heterologous molecules. [00229] In some embodiments, an antibody provided herein is conjugated to a second antibody to form an antibody heteroconjugate. [00230] In various embodiments, the antibody is genetically fused to the agent. Genetic fusion may be accomplished by placing a linker (e.g., a polypeptide) between the antibody and the agent. The linker may be a flexible linker. [00231] In various embodiments, the antibody is genetically conjugated to a therapeutic molecule, with a hinge region linking the antibody to the therapeutic molecule. [00232] Also provided herein are methods for making the various fusion proteins provided herein. The various methods described in Section 5.4 may also be utilized to make the fusion proteins provided herein. [00233] In a specific embodiment, the fusion protein provided herein is recombinantly expressed. Recombinant expression of a fusion protein provided herein may require construction of an expression vector containing a polynucleotide that encodes the protein or a fragment thereof. Once a polynucleotide encoding a protein provided herein or a fragment thereof has been obtained, the vector for the production of the molecule may be produced by recombinant DNA technology using techniques well-known in the art. Thus, methods for preparing a protein by expressing a polynucleotide containing an encoding nucleotide sequence are described herein. Methods which are well known to those skilled in the art can be used to construct expression vectors containing coding sequences and appropriate transcriptional and translational control signals. These methods include, for example, in vitro recombinant DNA techniques, synthetic techniques, and in vivo genetic recombination. Also provided are replicable vectors comprising a nucleotide sequence encoding a fusion protein provided herein, or a fragment thereof, or a CDR, operably linked to a promoter. [00234] The expression vector can be transferred to a host cell by conventional techniques and the transfected cells are then cultured by conventional techniques to produce a fusion protein provided herein. Thus, also provided herein are host cells containing a polynucleotide encoding a fusion protein provided herein or fragments thereof operably linked to a heterologous promoter. [00235] A variety of host-expression vector systems may be utilized to express the fusion protein provided herein. Such host-expression systems represent vehicles by which the coding sequences of interest may be produced and subsequently purified, but also represent cells which may, when transformed or transfected with the appropriate nucleotide coding sequences, express a fusion protein provided herein in situ. These include but are not limited to microorganisms such as bacteria (e.g., E. coli and B. subtilis) transformed with recombinant bacteriophage DNA, plasmid DNA or cosmid DNA expression vectors containing coding sequences; yeast (e.g., Saccharomyces Pichia) transformed with recombinant yeast expression vectors containing coding sequences; insect cell systems infected with recombinant virus expression vectors (e.g., baculovirus) containing coding sequences; plant cell systems infected with recombinant virus expression vectors (e.g., cauliflower mosaic virus, CaMV, tobacco mosaic virus, TMV) or transformed with recombinant plasmid expression vectors (e.g., Ti plasmid) containing coding sequences; or mammalian cell systems (e.g., COS, CHO, BHK, 293, NS0, and 3T3 cells) harboring recombinant expression constructs containing promoters derived from the genome of mammalian cells (e.g., metallothionein promoter) or from mammalian viruses (e.g., the adenovirus late promoter; the vaccinia virus 7.5K promoter). Bacterial cells such as Escherichia coli, or, eukaryotic cells, especially for the expression of whole recombinant antibody molecule, can be used for the expression of a recombinant fusion protein. For example, mammalian cells such as Chinese hamster ovary cells (CHO), in conjunction with a vector such as the major intermediate early gene promoter element from human cytomegalovirus is an effective expression system for antibodies or variants thereof. In a specific embodiment, the expression of nucleotide sequences encoding the fusion proteins provided herein is regulated by a constitutive promoter, inducible promoter or tissue specific promoter. [00236] In bacterial systems, a number of expression vectors may be advantageously selected depending upon the use intended for the fusion protein being expressed. For example, when a large quantity of such a fusion protein is to be produced, for the generation of pharmaceutical compositions of a fusion protein, vectors which direct the expression of high levels of fusion protein products that are readily purified may be desirable. Such vectors include, but are not limited to, the E. coli expression vector pUR278 (Ruther et al., EMBO 12:1791 (1983)), in which the coding sequence may be ligated individually into the vector in frame with the lac Z coding region so that a fusion protein is produced; pIN vectors (Inouye & Inouye, Nucleic Acids Res.13:3101-3109 (1985); Van Heeke & Schuster, J. Biol. Chem.24:5503-5509 (1989)); and the like. pGEX vectors may also be used to express foreign polypeptides as fusion proteins with glutathione 5-transferase (GST). In general, such fusion proteins are soluble and can easily be purified from lysed cells by adsorption and binding to matrix glutathione agarose beads followed by elution in the presence of free glutathione. The pGEX vectors are designed to include thrombin or factor Xa protease cleavage sites so that the cloned target gene product can be released from the GST moiety. [00237] In mammalian host cells, a number of viral-based expression systems may be utilized. In cases where an adenovirus is used as an expression vector, the coding sequence of interest may be ligated to an adenovirus transcription/translation control complex, e.g., the late promoter and tripartite leader sequence. This chimeric gene may then be inserted in the adenovirus genome by in vitro or in vivo recombination. Insertion in a non-essential region of the viral genome (e.g., region El or E3) will result in a recombinant virus that is viable and capable of expressing the fusion protein in infected hosts (e.g., see Logan & Shenk, Proc. Natl. Acad. Sci. USA 81:355-359 (1984)). Specific initiation signals may also be required for efficient translation of inserted coding sequences. These signals include the ATG initiation codon and adjacent sequences. Furthermore, the initiation codon must be in phase with the reading frame of the desired coding sequence to ensure translation of the entire insert. These exogenous translational control signals and initiation codons can be of a variety of origins, both natural and synthetic. The efficiency of expression may be enhanced by the inclusion of appropriate transcription enhancer elements, transcription terminators, etc. (see, e.g., Bittner et al., Methods in Enzymol.153:51-544 (1987)). [00238] In addition, a host cell strain may be chosen which modulates the expression of the inserted sequences, or modifies and processes the gene product in the specific fashion desired. Such modifications (e.g., glycosylation) and processing (e.g., cleavage) of protein products may be important for the function of the protein. Different host cells have characteristic and specific mechanisms for the post-translational processing and modification of proteins and gene products. Appropriate cell lines or host systems can be chosen to ensure the correct modification and processing of the foreign protein expressed. To this end, eukaryotic host cells which possess the cellular machinery for proper processing of the primary transcript, glycosylation, and phosphorylation of the gene product may be used. Such mammalian host cells include but are not limited to CHO, VERY, BHK, Hela, COS, MDCK, 293, 3T3, W138, BT483, Hs578T, HTB2, BT2O and T47D, NS0 (a murine myeloma cell line that does not endogenously produce any immunoglobulin chains), CRL7O3O and HsS78Bst cells. [00239] For long-term, high-yield production of recombinant proteins, stable expression can be utilized. For example, cell lines which stably express the fusion proteins may be engineered. Rather than using expression vectors which contain viral origins of replication, host cells can be transformed with DNA controlled by appropriate expression control elements (e.g., promoter, enhancer, sequences, transcription terminators, polyadenylation sites, etc.), and a selectable marker. Following the introduction of the foreign DNA, engineered cells may be allowed to grow for 1-2 days in an enriched media, and then are switched to a selective media. The selectable marker in the recombinant plasmid confers resistance to the selection and allows cells to stably integrate the plasmid into their chromosomes and grow to form foci which in turn can be cloned and expanded into cell lines. This method may advantageously be used to engineer cell lines which express the fusion protein. Such engineered cell lines may be particularly useful in screening and evaluation of compositions that interact directly or indirectly with the binding molecule. [00240] A number of selection systems may be used, including but not limited to, the herpes simplex virus thymidine kinase (Wigler et al., Cell 11:223 (1977)), hypoxanthineguanine phosphoribosyltransferase (Szybalska & Szybalski, Proc. Natl. Acad. Sci. USA 48:202 (1992)), and adenine phosphoribosyltransferase (Lowy et al., Cell 22:8-17 (1980)) genes can be employed in tk-, hgprt- or aprt-cells, respectively. Also, antimetabolite resistance can be used as the basis of selection for the following genes: dhfr, which confers resistance to methotrexate (Wigler et al., Natl. Acad. Sci. USA 77:357 (1980); O’Hare et al., Proc. Natl. Acad. Sci. USA 78:1527 (1981)); gpt, which confers resistance to mycophenolic acid (Mulligan & Berg, Proc. Natl. Acad. Sci. USA 78:2072 (1981)); neo, which confers resistance to the aminoglycoside G-418 (Wu and Wu, Biotherapy 3:87-95 (1991); Tolstoshev, Ann. Rev. Pharmacol. Toxicol.32:573-596 (1993); Mulligan, Science 260:926- 932 (1993); and Morgan and Anderson, Ann. Rev. Biochem.62:191-217 (1993); May, TIB TECH 11(5):l55-215 (1993)); and hygro, which confers resistance to hygromycin (Santerre et al., Gene 30:147 (1984)). Methods commonly known in the art of recombinant DNA technology may be routinely applied to select the desired recombinant clone, and such methods are described, for example, in Ausubel et al. (eds.), Current Protocols in Molecular Biology, John Wiley & Sons, NY (1993); Kriegler, Gene Transfer and Expression, A Laboratory Manual, Stockton Press, NY (1990); and in Chapters 12 and 13, Dracopoli et al. (eds.), Current Protocols in Human Genetics, John Wiley & Sons, NY (1994); Colberre-Garapin et al., J. Mol. Biol.150:1 (1981), which are incorporated by reference herein in their entireties. [00241] The expression level of a fusion protein can be increased by vector amplification (for a review, see Bebbington and Hentschel, The use of vectors based on gene amplification for the expression of cloned genes in mammalian cells in DNA cloning, Vol.3 (Academic Press, New York, 1987)). When a marker in the vector system expressing a fusion protein is amplifiable, increase in the level of inhibitor present in culture of host cell will increase the number of copies of the marker gene. Since the amplified region is associated with the fusion protein gene, production of the fusion protein will also increase (Crouse et al., Mol. Cell. Biol.3:257 (1983)). [00242] The host cell may be co-transfected with multiple expression vectors provided herein. The vectors may contain identical selectable markers which enable equal expression of respective encoding polypeptides. Alternatively, a single vector may be used which encodes, and is capable of expressing multiple polypeptides. The coding sequences may comprise cDNA or genomic DNA. [00243] Once a fusion protein provided herein has been produced by recombinant expression, it may be purified by any method known in the art for purification of a polypeptide (e.g., an immunoglobulin molecule), for example, by chromatography (e.g., ion exchange, affinity, particularly by affinity for the specific antigen after Protein A, sizing column chromatography, and Kappa select affinity chromatography), centrifugation, differential solubility, or by any other standard technique for the purification of proteins. Further, the fusion protein molecules provided herein can be fused to heterologous polypeptide sequences described herein or otherwise known in the art to facilitate purification. Immunoconjugates [00244] In some embodiments, the present disclosure also provides immunoconjugates comprising any of the anti-IL-23R antibodies described herein conjugated to one or more cytotoxic agents, such as chemotherapeutic agents or drugs, growth inhibitory agents, toxins (e.g., protein toxins, enzymatically active toxins of bacterial, fungal, plant, or animal origin, or fragments thereof), or radioactive isotopes. [00245] In some embodiments, an immunoconjugate is an antibody-drug conjugate (ADC) in which an antibody is conjugated to one or more drugs, including but not limited to a maytansinoid (see U.S. Patent Nos.5,208,020, 5,416,064 and European Patent EP 0425235 B1); an auristatin such as monomethylauristatin drug moieties DE and DF (MMAE and MMAF) (see U.S. Patent Nos. 5,635,483 and 5,780,588, and 7,498,298); a dolastatin; a calicheamicin or derivative thereof (see U.S. Patent Nos.5,712,374, 5,714,586, 5,739,116, 5,767,285, 5,770,701, 5,770,710, 5,773,001, and 5,877,296; Hinman et al., Cancer Res. 53:3336-3342 (1993); and Lode et al., Cancer Res.58:2925- 2928 (1998)); an anthracycline such as daunomycin or doxorubicin (see Kratz et al., Current Med. Chem.13:477-523 (2006); Jeffrey et al., Bioorganic & Med. Chem. Letters 16:358-362 (2006); Torgov et al., Bioconj. Chem.16:717-721 (2005); Nagy et al., Proc. Natl. Acad. Sci. USA 97:829-834 (2000); Dubowchik et al., Bioorg. & Med. Chem. Letters 12:1529-1532 (2002); King et al., J. Med. Chem.45:4336-4343 (2002); and U.S. Patent No.6,630,579); methotrexate; vindesine; a taxane such as docetaxel, paclitaxel, larotaxel, tesetaxel, and ortataxel; a trichothecene; and CC1065. [00246] In some embodiments, an immunoconjugate comprises an antibody as described herein conjugated to an enzymatically active toxin or fragment thereof, including but not limited to diphtheria A chain, nonbinding active fragments of diphtheria toxin, exotoxin A chain (from Pseudomonas aeruginosa), ricin A chain, abrin A chain, modeccin A chain, alpha-sarcin, Aleurites fordii proteins, dianthin proteins, Phytolaca americana proteins (PAPI, PAPII, and PAP-S), momordica charantia inhibitor, curcin, crotin, sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictocin, phenomycin, enomycin, and the tricothecenes. [00247] In some embodiments, an immunoconjugate comprises an antibody as described herein conjugated to a radioactive atom to form a radioconjugate. A variety of radioactive isotopes are available for the production of radioconjugates. Examples include At 211 , I 131 , I 125 , Y 90 , Re 186 , Re 188 , Sm 153 , Bi 212 , P 32 , Pb 212 and radioactive isotopes of Lu. When the radioconjugate is used for detection, it may comprise a radioactive atom for scintigraphic studies, for example tc99m or I123, or a spin label for nuclear magnetic resonance (NMR) imaging (also known as magnetic resonance imaging, mri), such as iodine-123 again, iodine-131, indium-111, fluorine-19, carbon-13, nitrogen-15, oxygen-17, gadolinium, manganese or iron. [00248] Conjugates of an antibody and cytotoxic agent may be made using a variety of bifunctional protein coupling agents such as N-succinimidyl-3-(2-pyridyldithio) propionate (SPDP), succinimidyl-4-(N-maleimidomethyl) cyclohexane-1-carboxylate (SMCC), iminothiolane (IT), bifunctional derivatives of imidoesters (such as dimethyl adipimidate HCl), active esters (such as disuccinimidyl suberate), aldehydes (such as glutaraldehyde), bis-azido compounds (such as bis (p- azidobenzoyl) hexanediamine), bis-diazonium derivatives (such as bis-(p-diazoniumbenzoyl)- ethylenediamine), diisocyanates (such as toluene 2,6-diisocyanate), and bis-active fluorine compounds (such as 1,5-difluoro-2,4-dinitrobenzene). For example, a ricin immunotoxin can be prepared as described in Vitetta et al., Science 238:1098 (1987). Carbon-14-labeled 1- isothiocyanatobenzyl-3-methyldiethylene triaminepentaacetic acid (MX-DTPA) is an exemplary chelating agent for conjugation of radionucleotide to the antibody. See WO94/11026. [00249] The linker may be a “cleavable linker” facilitating release of the conjugated agent in the cell, but non-cleavable linkers are also contemplated herein. Linkers for use in the conjugates of the present disclosure include, without limitation, acid labile linkers (e.g., hydrazone linkers), disulfide-containing linkers, peptidase-sensitive linkers (e.g., peptide linkers comprising amino acids, for example, valine and/or citrulline such as citrulline-valine or phenylalanine-lysine), photolabile linkers, dimethyl linkers, thioether linkers, or hydrophilic linkers designed to evade multidrug transporter-mediated resistance. [00250] The immunuoconjugates or ADCs herein contemplate, but are not limited to such conjugates prepared with cross-linker reagents including, but not limited to, BMPS, EMCS, GMBS, HBVS, LC-SMCC, MBS, MPBH, SBAP, SIA, SIAB, SMCC, SMPB, SMPH, sulfo-EMCS, sulfo- GMBS, sulfo-KMUS, sulfo-MBS, sulfo-SIAB, sulfo-SMCC, and sulfo-SMPB, and SVSB (succinimidyl-(4-vinylsulfone)benzoate) which are commercially available (e.g., from Pierce Biotechnology, Inc., Rockford, IL., U.S.A). [00251] In other embodiments, antibodies provided herein are conjugated or recombinantly fused, e.g., to a diagnostic molecule. Such diagnosis and detection can be accomplished, for example, by coupling the antibody to detectable substances including, but not limited to, various enzymes, such as, but not limited to, horseradish peroxidase, alkaline phosphatase, beta-galactosidase, or acetylcholinesterase; prosthetic groups, such as, but not limited to, streptavidin/biotin or avidin/biotin; fluorescent materials, such as, but not limited to, umbelliferone, fluorescein, fluorescein isothiocynate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride, or phycoerythrin; luminescent materials, such as, but not limited to, luminol; bioluminescent materials, such as, but not limited to, luciferase, luciferin, or aequorin; chemiluminescent material, such as, 225Acγ-emitting, Auger- emitting, β-emitting, an alpha-emitting or positron-emitting radioactive isotope. In some embodiments, the conjugated antibodies are used for screening purpose(s). In some embodiments, the screening method is high throughput screening with a library of the conjugated antibodies. In some embodiments, the conjugated antibodies are used to mark or label a cell or cellular target or antigen for diagnostic, screening, targeting, isolation, quantification or other such purposes or applications. In some embodiments, unique or distinct antibodies, including antibodies conjugated or fused to different diagnostic molecules may be utilized in combination in one or more such application, screening method, etc. Polynucleotides [00252] In certain embodiments, the disclosure provides polynucleotides that encode the present antibodies that bind to IL-23R and fusion proteins comprising the antibodies that bind to IL- 23R described herein. The polynucleotides of the disclosure can be in the form of RNA or in the form of DNA. DNA includes cDNA, genomic DNA, and synthetic DNA; and can be double-stranded or single-stranded, and if single stranded can be the coding strand or non-coding (anti-sense) strand. In some embodiments, the polynucleotide is in the form of cDNA. In some embodiments, the polynucleotide is a synthetic polynucleotide. [00253] The present disclosure further relates to variants of the polynucleotides described herein, wherein the variant encodes, for example, fragments, analogs, and/or derivatives of the antibody that binds IL-23R of the disclosure. In certain embodiments, the present disclosure provides a polynucleotide comprising a polynucleotide having a nucleotide sequence at least about 75% identical, at least about 80% identical, at least about 85% identical, at least about 90% identical, at least about 95% identical, and in some embodiments, at least about 96%, 97%, 98% or 99% identical to a polynucleotide encoding the antibody that binds IL-23R of the disclosure. As used herein, the phrase “a polynucleotide having a nucleotide sequence at least, for example, 95% “identical” to a reference nucleotide sequence” is intended to mean that the nucleotide sequence of the polynucleotide is identical to the reference sequence except that the polynucleotide sequence can include up to five point mutations per each 100 nucleotides of the reference nucleotide sequence. In other words, to obtain a polynucleotide having a nucleotide sequence at least 95% identical to a reference nucleotide sequence, up to 5% of the nucleotides in the reference sequence can be deleted or substituted with another nucleotide, or a number of nucleotides up to 5% of the total nucleotides in the reference sequence can be inserted into the reference sequence. These mutations of the reference sequence can occur at the 5′ or 3′ terminal positions of the reference nucleotide sequence or anywhere between those terminal positions, interspersed either individually among nucleotides in the reference sequence or in one or more contiguous groups within the reference sequence. [00254] The polynucleotide variants can contain alterations in the coding regions, non-coding regions, or both. In some embodiments, a polynucleotide variant contains alterations which produce silent substitutions, additions, or deletions, but does not alter the properties or activities of the encoded polypeptide. In some embodiments, a polynucleotide variant comprises silent substitutions that results in no change to the amino acid sequence of the polypeptide (due to the degeneracy of the genetic code). Polynucleotide variants can be produced for a variety of reasons, for example, to optimize codon expression for a particular host (i.e., change codons in the human mRNA to those preferred by a bacterial host such as E. coli). In some embodiments, a polynucleotide variant comprises at least one silent mutation in a non-coding or a coding region of the sequence. [00255] In some embodiments, a polynucleotide variant is produced to modulate or alter expression (or expression levels) of the encoded polypeptide. In some embodiments, a polynucleotide variant is produced to increase expression of the encoded polypeptide. In some embodiments, a polynucleotide variant is produced to decrease expression of the encoded polypeptide. In some embodiments, a polynucleotide variant has increased expression of the encoded polypeptide as compared to a parental polynucleotide sequence. In some embodiments, a polynucleotide variant has decreased expression of the encoded polypeptide as compared to a parental polynucleotide sequence. [00256] Also provided are vectors comprising the nucleic acid molecules described herein. In an embodiment, the nucleic acid molecules can be incorporated into a recombinant expression vector. The present disclosure provides recombinant expression vectors comprising any of the nucleic acids of the disclosure. As used herein, the term “recombinant expression vector” means a genetically- modified oligonucleotide or polynucleotide construct that permits the expression of an mRNA, protein, polypeptide, or peptide by a host cell, when the construct comprises a nucleotide sequence encoding the mRNA, protein, polypeptide, or peptide, and the vector is contacted with the cell under conditions sufficient to have the mRNA, protein, polypeptide, or peptide expressed within the cell. The vectors described herein are not naturally-occurring as a whole; however, parts of the vectors can be naturally-occurring. The described recombinant expression vectors can comprise any type of nucleotides, including, but not limited to DNA and RNA, which can be single-stranded or double- stranded, synthesized or obtained in part from natural sources, and which can contain natural, non- natural or altered nucleotides. The recombinant expression vectors can comprise naturally-occurring or non-naturally-occurring internucleotide linkages, or both types of linkages. The non-naturally occurring or altered nucleotides or internucleotide linkages do not hinder the transcription or replication of the vector. [00257] In an embodiment, the recombinant expression vector of the disclosure can be any suitable recombinant expression vector, and can be used to transform or transfect any suitable host. Suitable vectors include those designed for propagation and expansion or for expression or both, such as plasmids and viruses. The vector can be selected from the group consisting of the pUC series (Fermentas Life Sciences, Glen Burnie, Md.), the pBluescript series (Stratagene, LaJolla, Calif.), the pET series (Novagen, Madison, Wis.), the pGEX series (Pharmacia Biotech, Uppsala, Sweden), and the pEX series (Clontech, Palo Alto, Calif.). Bacteriophage vectors, such as λGT10, λGT11, λEMBL4, and λNM1149, λZapII (Stratagene) can be used. Examples of plant expression vectors include pBI01, pBI01.2, pBI121, pBI101.3, and pBIN19 (Clontech). Examples of animal expression vectors include pEUK-Cl, pMAM, and pMAMneo (Clontech). The recombinant expression vector may be a viral vector, e.g., a retroviral vector, e.g., a gamma retroviral vector. [00258] In an embodiment, the recombinant expression vectors are prepared using standard recombinant DNA techniques described in, for example, Sambrook et al., supra, and Ausubel et al., supra. Constructs of expression vectors, which are circular or linear, can be prepared to contain a replication system functional in a prokaryotic or eukaryotic host cell. Replication systems can be derived, e.g., from ColE1, SV40, 2µ plasmid, λ, bovine papilloma virus, and the like. [00259] The recombinant expression vector may comprise regulatory sequences, such as transcription and translation initiation and termination codons, which are specific to the type of host (e.g., bacterium, plant, fungus, or animal) into which the vector is to be introduced, as appropriate, and taking into consideration whether the vector is DNA- or RNA-based. [00260] The recombinant expression vector can include one or more marker genes, which allow for selection of transformed or transfected hosts. Marker genes include biocide resistance, e.g., resistance to antibiotics, heavy metals, etc., complementation in an auxotrophic host to provide prototrophy, and the like. Suitable marker genes for the described expression vectors include, for instance, neomycin/G418 resistance genes, histidinol x resistance genes, histidinol resistance genes, tetracycline resistance genes, and ampicillin resistance genes. [00261] The recombinant expression vector can comprise a native or normative promoter operably linked to the nucleotide sequence of the disclosure. The selection of promoters, e.g., strong, weak, tissue-specific, inducible and developmental-specific, is within the ordinary skill of the artisan. Similarly, the combining of a nucleotide sequence with a promoter is also within the skill of the artisan. The promoter can be a non-viral promoter or a viral promoter, e.g., a cytomegalovirus (CMV) promoter, an RSV promoter, an SV40 promoter, or a promoter found in the long-terminal repeat of the murine stem cell virus. [00262] The recombinant expression vectors can be designed for either transient expression, for stable expression, or for both. Also, the recombinant expression vectors can be made for constitutive expression or for inducible expression. [00263] Further, the recombinant expression vectors can be made to include a suicide gene. As used herein, the term “suicide gene” refers to a gene that causes the cell expressing the suicide gene to die. The suicide gene can be a gene that confers sensitivity to an agent, e.g., a drug, upon the cell in which the gene is expressed, and causes the cell to die when the cell is contacted with or exposed to the agent. Suicide genes are known in the art and include, for example, the Herpes Simplex Virus (HSV) thymidine kinase (TK) gene, cytosine deaminase, purine nucleoside phosphorylase, and nitroreductase. [00264] In certain embodiments, a polynucleotide is isolated. In certain embodiments, a polynucleotide is substantially pure. [00265] Also provided are host cells comprising the nucleic acid molecules described herein. The host cell may be any cell that contains a heterologous nucleic acid. The heterologous nucleic acid can be a vector (e.g., an expression vector). For example, a host cell can be a cell from any organism that is selected, modified, transformed, grown, used or manipulated in any way, for the production of a substance by the cell, for example the expression by the cell of a gene, a DNA or RNA sequence, a protein or an enzyme. An appropriate host may be determined. For example, the host cell may be selected based on the vector backbone and the desired result. By way of example, a plasmid or cosmid can be introduced into a prokaryote host cell for replication of several types of vectors. Bacterial cells such as, but not limited to DH5α, JM109, and KCB, SURE® Competent Cells, and SOLOPACK Gold Cells, can be used as host cells for vector replication and/or expression. Additionally, bacterial cells such as E. coli LE392 could be used as host cells for phage viruses. Eukaryotic cells that can be used as host cells include, but are not limited to yeast (e.g., YPH499, YPH500 and YPH501), insects and mammals. Examples of mammalian eukaryotic host cells for replication and/or expression of a vector include, but are not limited to, HeLa, NIH3T3, Jurkat, 293, COS, Saos, PC12, SP2/0 (American Type Culture Collection (ATCC), Manassas, VA, CRL-1581), NS0 (European Collection of Cell Cultures (ECACC), Salisbury, Wiltshire, UK, ECACC No. 85110503), FO (ATCC CRL-1646) and Ag653 (ATCC CRL-1580) murine cell lines. An exemplary human myeloma cell line is U266 (ATCC CRL-TIB-196). Other useful cell lines include those derived from Chinese Hamster Ovary (CHO) cells such as CHO-K1SV (Lonza Biologics, Walkersville, MD), CHO-K1 (ATCC CRL-61) or DG44. Preparation of Antibodies and Method of Making [00266] Methods of preparing antibodies have been described. See, e.g., Els Pardon et al, Nature Protocol, 9(3): 674 (2014). Antibodies (such as scFv fragments) may be obtained using methods known in the art such as by immunizing a Camelid species (such as camel or llama) and obtaining hybridomas therefrom, or by cloning a library of antibodies using molecular biology techniques known in the art and subsequent selection by ELISA with individual clones of unselected libraries or by using phage display. [00267] Antibodies provided herein may be produced by culturing cells transformed or transfected with a vector containing an antibody-encoding nucleic acid. Polynucleotide sequences encoding polypeptide components of the antibody of the present disclosure can be obtained using standard recombinant techniques. Desired polynucleotide sequences may be isolated and sequenced from antibody producing cells such as hybridomas cells or B cells. Alternatively, polynucleotides can be synthesized using nucleotide synthesizer or PCR techniques. Once obtained, sequences encoding the polypeptides are inserted into a recombinant vector capable of replicating and expressing heterologous polynucleotides in host cells. Many vectors that are available and known in the art can be used for the purpose of the present disclosure. Selection of an appropriate vector will depend mainly on the size of the nucleic acids to be inserted into the vector and the particular host cell to be transformed with the vector. Host cells suitable for expressing antibodies of the present disclosure include prokaryotes such as Archaebacteria and Eubacteria, including Gram-negative or Gram- positive organisms, eukaryotic microbes such as filamentous fungi or yeast, invertebrate cells such as insect or plant cells, and vertebrate cells such as mammalian host cell lines. Host cells are transformed with the above-described expression vectors and cultured in conventional nutrient media modified as appropriate for inducing promoters, selecting transformants, or amplifying the genes encoding the desired sequences. Antibodies produced by the host cells are purified using standard protein purification methods as known in the art. [00268] Methods for antibody production including vector construction, expression, and purification are further described in Plückthun et al., Antibody Engineering: Producing antibodies in Escherichia coli: From PCR to fermentation 203-52 (McCafferty et al. eds., 1996); Kwong and Rader, E. coli Expression and Purification of Fab Antibody Fragments, in Current Protocols in Protein Science (2009); Tachibana and Takekoshi, Production of Antibody Fab Fragments in Escherichia coli, in Antibody Expression and Production (Al-Rubeai ed., 2011); and Therapeutic Monoclonal Antibodies: From Bench to Clinic (An ed., 2009). [00269] It is, of course, contemplated that alternative methods, which are well known in the art, may be employed to prepare anti-IL-23R antibodies. For instance, the appropriate amino acid sequence, or portions thereof, may be produced by direct peptide synthesis using solid-phase techniques (see, e.g., Stewart et al., Solid-Phase Peptide Synthesis (1969); and Merrifield, J. Am. Chem. Soc.85:2149-54 (1963)). In vitro protein synthesis may be performed using manual techniques or by automation. Various portions of the anti-IL-23R antibody may be chemically synthesized separately and combined using chemical or enzymatic methods to produce the desired anti-IL-23R antibody. Alternatively, antibodies may be purified from cells or bodily fluids, such as milk, of a transgenic animal engineered to express the antibody, as disclosed, for example, in U.S. Pat. Nos.5,545,807 and 5,827,690. Polyclonal Antibodies [00270] Polyclonal antibodies are generally raised in animals by multiple subcutaneous (sc) or intraperitoneal (ip) injections of the relevant antigen and an adjuvant. It may be useful to conjugate the relevant antigen to a protein that is immunogenic in the species to be immunized, e.g., keyhole limpet hemocyanin (KLH), serum albumin, bovine thyroglobulin, or soybean trypsin inhibitor, using a bifunctional or derivatizing agent, e.g., maleimidobenzoyl sulfosuccinimide ester (conjugation through cysteine residues), N-hydroxysuccinimide (through lysine residues), glutaraldehyde, succinic anhydride, SOCl2, or R 1 N═C═NR, where R and R 1 are independently lower alkyl groups. Examples of adjuvants which may be employed include Freund's complete adjuvant and MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate). The immunization protocol may be selected by one skilled in the art without undue experimentation. [00271] For example, the animals are immunized against the antigen, immunogenic conjugates, or derivatives by combining, e.g., 100 µg or 5 µg of the protein or conjugate (for rabbits or mice, respectively) with 3 volumes of Freund's complete adjuvant and injecting the solution intradermally at multiple sites. One month later, the animals are boosted with 1/5 to 1/10 the original amount of peptide or conjugate in Freund's complete adjuvant by subcutaneous injection at multiple sites. Seven to fourteen days later, the animals are bled and the serum is assayed for antibody titer. Animals are boosted until the titer plateaus. Conjugates also can be made in recombinant cell culture as protein fusions. Also, aggregating agents such as alum are suitable to enhance the immune response. Monoclonal Antibodies [00272] Monoclonal antibodies are obtained from a population of substantially homogeneous antibodies, i.e., the individual antibodies comprising the population are identical except for possible naturally occurring mutations and/or post-translational modifications (e.g., isomerizations, amidations) that may be present in minor amounts. Thus, the modifier “monoclonal” indicates the character of the antibody as not being a mixture of discrete antibodies. [00273] For example, the monoclonal antibodies may be made using the hybridoma method first described by Kohler et al., Nature, 256:495 (1975), or may be made by recombinant DNA methods (U.S. Pat. No.4,816,567). [00274] In the hybridoma method, an appropriate host animal is immunized to elicit lymphocytes that produce or are capable of producing antibodies that will specifically bind the protein used for immunization. Alternatively, lymphocytes may be immunized in vitro. Lymphocytes then are fused with myeloma cells using a suitable fusing agent, such as polyethylene glycol, to form a hybridoma cell (Goding, Monoclonal Antibodies: Principles and Practice, pp.59-103 (Academic Press, 1986). [00275] The immunizing agent will typically include the antigenic protein or a fusion variant thereof. Goding, Monoclonal Antibodies: Principles and Practice, Academic Press (1986), pp.59- 103. Immortalized cell lines are usually transformed mammalian cells. The hybridoma cells thus prepared are seeded and grown in a suitable culture medium that preferably contains one or more substances that inhibit the growth or survival of the unfused, parental myeloma cells. Preferred immortalized myeloma cells are those that fuse efficiently, support stable high-level production of antibody by the selected antibody-producing cells, and are sensitive to a medium such as HAT medium. [00276] Culture medium in which hybridoma cells are growing is assayed for production of monoclonal antibodies directed against the antigen. The culture medium in which the hybridoma cells are cultured can be assayed for the presence of monoclonal antibodies directed against the desired antigen. Such techniques and assays are known in the in art. For example, binding affinity may be determined by the Scatchard analysis of Munson et al., Anal. Biochem., 107:220 (1980). [00277] After hybridoma cells are identified that produce antibodies of the desired specificity, affinity, and/or activity, the clones may be subcloned by limiting dilution procedures and grown by standard methods (Goding, supra). Suitable culture media for this purpose include, for example, D- MEM or RPMI-1640 medium. In addition, the hybridoma cells may be grown in vivo as tumors in a mammal. [00278] The monoclonal antibodies secreted by the subclones are suitably separated from the culture medium, ascites fluid, or serum by conventional immunoglobulin purification procedures such as, for example, protein A-Sepharose, hydroxylapatite chromatography, gel electrophoresis, dialysis, or affinity chromatography. [00279] Monoclonal antibodies may also be made by recombinant DNA methods, such as those described in U.S. Pat. No.4,816,567, and as described above. DNA encoding the monoclonal antibodies is readily isolated and sequenced using conventional procedures (e.g., by using oligonucleotide probes that are capable of binding specifically to genes encoding the heavy and light chains of murine antibodies). The hybridoma cells serve as a preferred source of such DNA. Once isolated, the DNA may be placed into expression vectors, which are then transfected into host cells such as E. coli cells, simian COS cells, Chinese hamster ovary (CHO) cells, or myeloma cells that do not otherwise produce immunoglobulin protein, in order to synthesize monoclonal antibodies in such recombinant host cells. Review articles on recombinant expression in bacteria of DNA encoding the antibody include Skerra et al., Curr. Opinion in Immunol., 5:256-262 (1993) and Pliickthun, Immunol. Revs.130:151-188 (1992). [00280] In a further embodiment, antibodies can be isolated from antibody phage libraries generated using the techniques described in McCafferty et al., Nature, 348:552-554 (1990). Clackson et al., Nature, 352:624-628 (1991) and Marks et al., J. Mol. Biol., 222:581-597 (1991). Subsequent publications describe the production of high affinity (nM range) human antibodies by chain shuffling (Marks et al., Bio/Technology, 10:779-783 (1992)), as well as combinatorial infection and in vivo recombination as a strategy for constructing very large phage libraries (Waterhouse et al., Nucl. Acids Res., 21:2265-2266 (1993)). Thus, these techniques are viable alternatives to traditional monoclonal antibody hybridoma techniques for isolation of monoclonal antibodies. [00281] The DNA also may be modified, for example, by substituting the coding sequence (U.S. Pat. No.4,816,567; Morrison, et al., Proc. Natl Acad. Sci. USA, 81:6851 (1984)), or by covalently joining to the coding sequence all or part of the coding sequence for a non- immunoglobulin polypeptide. Such non-immunoglobulin polypeptides can be substituted to create a chimeric bivalent antibody comprising one antigen-combining site having specificity for an antigen and another antigen-combining site having specificity for a different antigen. [00282] Chimeric or hybrid antibodies also may be prepared in vitro using known methods in synthetic protein chemistry, including those involving crosslinking agents. For example, immunotoxins may be constructed using a disulfide-exchange reaction or by forming a thioether bond. Examples of suitable reagents for this purpose include iminothiolate and methyl-4- mercaptobutyrimidate. Recombinant Production in Prokaryotic Cells [00283] Polynucleic acid sequences encoding the antibodies of the present disclosure can be obtained using standard recombinant techniques. Desired polynucleic acid sequences may be isolated and sequenced from antibody producing cells such as hybridoma cells. Alternatively, polynucleotides can be synthesized using nucleotide synthesizer or PCR techniques. Once obtained, sequences encoding the polypeptides are inserted into a recombinant vector capable of replicating and expressing heterologous polynucleotides in prokaryotic hosts. Many vectors that are available and known in the art can be used for the purpose of the present disclosure. Selection of an appropriate vector will depend mainly on the size of the nucleic acids to be inserted into the vector and the particular host cell to be transformed with the vector. Each vector contains various components, depending on its function (amplification or expression of heterologous polynucleotide, or both) and its compatibility with the particular host cell in which it resides. The vector components generally include, but are not limited to, an origin of replication, a selection marker gene, a promoter, a ribosome binding site (RBS), a signal sequence, the heterologous nucleic acid insert and a transcription termination sequence. [00284] In general, plasmid vectors containing replicon and control sequences which are derived from species compatible with the host cell are used in connection with these hosts. The vector ordinarily carries a replication site, as well as marking sequences which are capable of providing phenotypic selection in transformed cells. For example, E. coli is typically transformed using pBR322, a plasmid derived from an E. coli species. Examples of pBR322 derivatives used for expression of particular antibodies are described in detail in Carter et al., U.S. Pat. No.5,648,237. [00285] In addition, phage vectors containing replicon and control sequences that are compatible with the host microorganism can be used as transforming vectors in connection with these hosts. For example, bacteriophage such as GEM™-11 may be utilized in making a recombinant vector which can be used to transform susceptible host cells such as E. coli LE392. [00286] The expression vector of the present application may comprise two or more promoter-cistron pairs, encoding each of the polypeptide components. A promoter is an untranslated regulatory sequence located upstream (5′) to a cistron that modulates its expression. Prokaryotic promoters typically fall into two classes, inducible and constitutive. Inducible promoter is a promoter that initiates increased levels of transcription of the cistron under its control in response to changes in the culture condition, e.g. the presence or absence of a nutrient or a change in temperature. [00287] A large number of promoters recognized by a variety of potential host cells are well known. The selected promoter can be operably linked to cistron DNA encoding the present antibody by removing the promoter from the source DNA via restriction enzyme digestion and inserting the isolated promoter sequence into the vector of the present application. Both the native promoter sequence and many heterologous promoters may be used to direct amplification and/or expression of the target genes. In some embodiments, heterologous promoters are utilized, as they generally permit greater transcription and higher yields of expressed target gene as compared to the native target polypeptide promoter. [00288] Promoters suitable for use with prokaryotic hosts include the PhoA promoter, the - galactamase and lactose promoter systems, a tryptophan (trp) promoter system and hybrid promoters such as the tac or the trc promoter. However, other promoters that are functional in bacteria (such as other known bacterial or phage promoters) are suitable as well. Their nucleic acid sequences have been published, thereby enabling a skilled worker operably to ligate them to cistrons encoding the target peptide (Siebenlist et al. Cell 20: 269 (1980)) using linkers or adaptors to supply any required restriction sites. [00289] In one aspect, each cistron within the recombinant vector comprises a secretion signal sequence component that directs translocation of the expressed polypeptides across a membrane. In general, the signal sequence may be a component of the vector, or it may be a part of the target polypeptide DNA that is inserted into the vector. The signal sequence selected for the purpose of this invention should be one that is recognized and processed (i.e. cleaved by a signal peptidase) by the host cell. For prokaryotic host cells that do not recognize and process the signal sequences native to the heterologous polypeptides, the signal sequence can be substituted by a prokaryotic signal sequence selected, for example, from the group consisting of the alkaline phosphatase, penicillinase, Ipp, or heat-stable enterotoxin II (STII) leaders, LamB, PhoE, PelB, OmpA and MBP. [00290] In some embodiments, the production of the antibodies according to the present disclosure can occur in the cytoplasm of the host cell, and therefore does not require the presence of secretion signal sequences within each cistron. Certain host strains (e.g., the E. coli trxB − strains) provide cytoplasm conditions that are favorable for disulfide bond formation, thereby permitting proper folding and assembly of expressed protein subunits. [00291] Prokaryotic host cells suitable for expressing the antibodies of the present disclosure include Archaebacteria and Eubacteria, such as Gram-negative or Gram-positive organisms. Examples of useful bacteria include Escherichia (e.g., E. coli), Bacilli (e.g., B. subtilis), Enterobacteria, Pseudomonas species (e.g., P. aeruginosa), Salmonella typhimurium, Serratia marcescans, Klebsiella, Proteus, Shigella, Rhizobia, Vitreoscilla, or Paracoccus. In some embodiments, gram-negative cells are used. In one embodiment, E. coli cells are used as hosts. Examples of E. coli strains include strain W3110 (Bachmann, Cellular and Molecular Biology, vol.2 (Washington, D.C.: American Society for Microbiology, 1987), pp.1190-1219; ATCC Deposit No. 27,325) and derivatives thereof, including strain 33D3 having genotype W3110 AfhuA (AtonA) ptr3 lac Iq lacL8 AompT A(nmpc-fepE) degP41 kan R (U.S. Pat. No.5,639,635). Other strains and derivatives thereof, such as E. coli 294 (ATCC 31,446), E. coli B, E. coli 1776 (ATCC 31,537) and E. coli RV308 (ATCC 31,608) are also suitable. These examples are illustrative rather than limiting. Methods for constructing derivatives of any of the above-mentioned bacteria having defined genotypes are known in the art and described in, for example, Bass et al., Proteins, 8:309-314 (1990). It is generally necessary to select the appropriate bacteria taking into consideration replicability of the replicon in the cells of a bacterium. For example, E. coli, Serratia, or Salmonella species can be suitably used as the host when well known plasmids such as pBR322, pBR325, pACYC177, or pKN410 are used to supply the replicon. [00292] Typically the host cell should secrete minimal amounts of proteolytic enzymes, and additional protease inhibitors may desirably be incorporated in the cell culture. [00293] Host cells are transformed with the above-described expression vectors and cultured in conventional nutrient media modified as appropriate for inducing promoters, selecting transformants, or amplifying the genes encoding the desired sequences. Transformation means introducing DNA into the prokaryotic host so that the DNA is replicable, either as an extrachromosomal element or by chromosomal integrant. Depending on the host cell used, transformation is done using standard techniques appropriate to such cells. The calcium treatment employing calcium chloride is generally used for bacterial cells that contain substantial cell-wall barriers. Another method for transformation employs polyethylene glycol/DMSO. Yet another technique used is electroporation. [00294] Prokaryotic cells used to produce the antibodies of the present application are grown in media known in the art and suitable for culture of the selected host cells. Examples of suitable media include luria broth (LB) plus necessary nutrient supplements. In some embodiments, the media also contains a selection agent, chosen based on the construction of the expression vector, to selectively permit growth of prokaryotic cells containing the expression vector. For example, ampicillin is added to media for growth of cells expressing ampicillin resistant gene. [00295] Any necessary supplements besides carbon, nitrogen, and inorganic phosphate sources may also be included at appropriate concentrations introduced alone or as a mixture with another supplement or medium such as a complex nitrogen source. Optionally the culture medium may contain one or more reducing agents selected from the group consisting of glutathione, cysteine, cystamine, thioglycollate, dithioerythritol and dithiothreitol. The prokaryotic host cells are cultured at suitable temperatures and pHs. [00296] If an inducible promoter is used in the expression vector of the present application, protein expression is induced under conditions suitable for the activation of the promoter. In one aspect of the present application, PhoA promoters are used for controlling transcription of the polypeptides. Accordingly, the transformed host cells are cultured in a phosphate-limiting medium for induction. In some embodiments, the phosphate-limiting medium is the C.R.A.P medium (see, e.g., Simmons et al., J. Immunol. Methods 263:133-147 (2002)). A variety of other inducers may be used, according to the vector construct employed, as is known in the art. [00297] The expressed antibodies of the present disclosure are secreted into and recovered from the periplasm of the host cells. Protein recovery typically involves disrupting the microorganism, generally by such means as osmotic shock, sonication or lysis. Once cells are disrupted, cell debris or whole cells may be removed by centrifugation or filtration. The proteins may be further purified, for example, by affinity resin chromatography. Alternatively, proteins can be transported into the culture media and isolated therein. Cells may be removed from the culture and the culture supernatant being filtered and concentrated for further purification of the proteins produced. The expressed polypeptides can be further isolated and identified using commonly known methods such as polyacrylamide gel electrophoresis (PAGE) and Western blot assay. [00298] Alternatively, protein production is conducted in large quantity by a fermentation process. Various large-scale fed-batch fermentation procedures are available for production of recombinant proteins. To improve the production yield and quality of the antibodies of the present disclosure, various fermentation conditions can be modified. For example, the chaperone proteins have been demonstrated to facilitate the proper folding and solubility of heterologous proteins produced in bacterial host cells. Chen et al. J Bio Chem 274:19601-19605 (1999); U.S. Pat. No. 6,083,715; U.S. Pat. No.6,027,888; Bothmann and Pluckthun, J. Biol. Chem.275:17100-17105 (2000); Ramm and Pluckthun, J. Biol. Chem.275:17106-17113 (2000); Arie et al., Mol. Microbiol. 39:199-210 (2001). [00299] To minimize proteolysis of expressed heterologous proteins (especially those that are proteolytically sensitive), certain host strains deficient for proteolytic enzymes can be used for the present invention, as described in, for example, U.S. Pat. No.5,264,365; U.S. Pat. No.5,508,192; Hara et al., Microbial Drug Resistance, 2:63-72 (1996). E. coli strains deficient for proteolytic enzymes and transformed with plasmids overexpressing one or more chaperone proteins may be used as host cells in the expression system encoding the antibodies of the present application. [00300] The antibodies produced herein can be further purified to obtain preparations that are substantially homogeneous for further assays and uses. Standard protein purification methods known in the art can be employed. The following procedures are exemplary of suitable purification procedures: fractionation on immunoaffinity or ion-exchange columns, ethanol precipitation, reverse phase HPLC, chromatography on silica or on a cation-exchange resin such as DEAE, chromatofocusing, SDS-PAGE, ammonium sulfate precipitation, and gel filtration using, for example, Sephadex G-75. Protein A immobilized on a solid phase for example can be used in some embodiments for immunoaffinity purification of binding molecules of the present disclosure. In some embodiments, the solid phase to which Protein A is immobilized is a column comprising a glass or silica surface. In some embodiments, the solid phase to which Protein A is immobilized is a controlled pore glass column or a silicic acid column. In some embodiments, the column has been coated with a reagent, such as glycerol, in an attempt to prevent nonspecific adherence of contaminants. The solid phase is then washed to remove contaminants non-specifically bound to the solid phase. Finally the antibodies of interest is recovered from the solid phase by elution. Recombinant Production in Eukaryotic Cells [00301] For eukaryotic expression, the vector components generally include, but are not limited to, one or more of the following, a signal sequence, an origin of replication, one or more marker genes, and enhancer element, a promoter, and a transcription termination sequence. [00302] A vector for use in a eukaryotic host may also an insert that encodes a signal sequence or other polypeptide having a specific cleavage site at the N-terminus of the mature protein or polypeptide. The heterologous signal sequence selected preferably is one that is recognized and processed (i.e., cleaved by a signal peptidase) by the host cell. In mammalian cell expression, mammalian signal sequences as well as viral secretory leaders, for example, the herpes simplex gD signal, are available. The DNA for such precursor region can be ligated in reading frame to DNA encoding the antibodies of the present application. [00303] Generally, the origin of replication component is not needed for mammalian expression vectors (the SV40 origin may typically be used only because it contains the early promoter). [00304] Expression and cloning vectors may contain a selection gene, also termed a selectable marker. Selection genes may encode proteins that confer resistance to antibiotics or other toxins, e.g., ampicillin, neomycin, methotrexate, or tetracycline; complement auxotrophic deficiencies; or supply critical nutrients not available from complex media. [00305] One example of a selection scheme utilizes a drug to arrest growth of a host cell. Those cells that are successfully transformed with a heterologous gene produce a protein conferring drug resistance and thus survive the selection regimen. Examples of such dominant selection use the drugs neomycin, mycophenolic acid and hygromycin. [00306] Another example of suitable selectable markers for mammalian cells are those that enable the identification of cells competent to take up nucleic acid encoding the antibodies of the present application. For example, cells transformed with the DHFR selection gene are first identified by culturing all of the transformants in a culture medium that contains methotrexate (Mtx), a competitive antagonist of DHFR. An exemplary appropriate host cell when wild-type DHFR is employed is the Chinese hamster ovary (CHO) cell line deficient in DHFR activity. Alternatively, host cells (particularly wild-type hosts that contain endogenous DHFR) transformed or co- transformed with the polypeptide encoding-DNA sequences, wild-type DHFR protein, and another selectable marker such as aminoglycoside 3′-phosphotransferase (APH) can be selected by cell growth in medium containing a selection agent for the selectable marker such as an aminoglycosidic antibiotic. [00307] Expression and cloning vectors usually contain a promoter that is recognized by the host organism and is operably linked to the nucleic acid encoding the desired polypeptide sequences. Eukaryotic genes have an AT-rich region located approximately 25 to 30 based upstream from the site where transcription is initiated. Another sequence found 70 to 80 bases upstream from the start of the transcription of many genes may be included. The 3′ end of most eukaryotic may be the signal for addition of the poly A tail to the 3′ end of the coding sequence. All of these sequences may be inserted into eukaryotic expression vectors. [00308] Polypeptide transcription from vectors in mammalian host cells can be controlled, for example, by promoters obtained from the genomes of viruses such as polyoma virus, fowlpox virus, adenovirus (such as Adenovirus 2), bovine papilloma virus, avian sarcoma virus, cytomegalovirus, a retrovirus, hepatitis-B virus and Simian Virus 40 (SV40), from heterologous mammalian promoters, e.g., the actin promoter or an immunoglobulin promoter, from heat-shock promoters, provided such promoters are compatible with the host cell systems. [00309] Transcription of a DNA encoding the antibodies of the present disclosure by higher eukaryotes is often increased by inserting an enhancer sequence into the vector. Many enhancer sequences are now known from mammalian genes (globin, elastase, albumin, α-fetoprotein, and insulin). Examples include the SV40 enhancer on the late side of the replication origin (bp 100-270), the cytomegalovirus early promoter enhancer, the polyoma enhancer on the late side of the replication origin, and adenovirus enhancers. See also Yaniv, Nature 297:17-18 (1982) on enhancing elements for activation of eukaryotic promoters. The enhancer may be spliced into the vector at a position 5′ or 3′ to the polypeptide encoding sequence, but is preferably located at a site 5′ from the promoter. [00310] Expression vectors used in eukaryotic host cells (yeast, fungi, insect, plant, animal, human, or nucleated cells from other multicellular organisms) also contain sequences necessary for the termination of transcription and for stabilizing the mRNA. Such sequences are commonly available from the 5′ and, occasionally 3′, untranslated regions of eukaryotic or viral DNAs or cDNAs. These regions contain nucleotide segments transcribed as polyadenylated fragments in the untranslated portion of the polypeptide-encoding mRNA. One useful transcription termination component is the bovine growth hormone polyadenylation region. [00311] Suitable host cells for cloning or expressing the DNA in the vectors herein include higher eukaryote cells described herein, including vertebrate host cells. Propagation of vertebrate cells in culture (tissue culture) has become a routine procedure. Examples of useful mammalian host cell lines are monkey kidney CV1 line transformed by SV40 (COS-7, ATCC CRL 1651); human embryonic kidney line (293 or 293 cells subcloned for growth in suspension culture, Graham et al., J. Gen Virol.36:59 (1977)); baby hamster kidney cells (BHK, ATCC CCL 10); Chinese hamster ovary cells/−DHFR (CHO, Urlaub et al., Proc. Natl. Acad. Sci. USA 77:4216 (1980)); mouse sertoli cells (TM4, Mather, Biol. Reprod.23:243-251 (1980)); monkey kidney cells (CV1 ATCC CCL 70); African green monkey kidney cells (VERO-76, ATCC CRL-1587); human cervical carcinoma cells (HELA, ATCC CCL 2); canine kidney cells (MDCK, ATCC CCL 34); buffalo rat liver cells (BRL 3A, ATCC CRL 1442); human lung cells (W138, ATCC CCL 75); human liver cells (Hep G2, HB 8065); mouse mammary tumor (MMT 060562, ATCC CCL51); TR1 cells (Mather et al., Annals N.Y. Acad. Sci.383:44-68 (1982)); MRC 5 cells; FS4 cells; and a human hepatoma line (Hep G2). [00312] Host cells can be transformed with the above-described expression or cloning vectors for antibodies production and cultured in conventional nutrient media modified as appropriate for inducing promoters, selecting transformants, or amplifying the genes encoding the desired sequences. [00313] The host cells used to produce the antibodies of the present application may be cultured in a variety of media. Commercially available media such as Ham's F10 (Sigma), Minimal Essential Medium ((MEM), (Sigma), RPMI-1640 (Sigma), and Dulbecco's Modified Eagle's Medium ((DMEM), Sigma) are suitable for culturing the host cells. In addition, any of the media described in Ham et al., Meth. Enz.58:44 (1979), Barnes et al., Anal. Biochem.102:255 (1980), U.S. Pat. No. 4,767,704; 4,657,866; 4,927,762; 4,560,655; or 5,122,469; WO 90/03430; WO 87/00195; or U.S. Pat. Re.30,985 may be used as culture media for the host cells. Any of these media may be supplemented as necessary with hormones and/or other growth factors (such as insulin, transferrin, or epidermal growth factor), salts (such as sodium chloride, calcium, magnesium, and phosphate), buffers (such as HEPES), nucleotides (such as adenosine and thymidine), antibiotics (such as GENTAMYCIN™ drug), trace elements (defined as inorganic compounds usually present at final concentrations in the micromolar range), and glucose or an equivalent energy source. Any other necessary supplements may also be included at appropriate concentrations that would be known to those skilled in the art. The culture conditions, such as temperature, pH, and the like, are those previously used with the host cell selected for expression, and will be apparent to the ordinarily skilled artisan. [00314] When using recombinant techniques, the antibodies can be produced intracellularly, in the periplasmic space, or directly secreted into the medium. If the antibody is produced intracellularly, as a first step, the particulate debris, either host cells or lysed fragments, are removed, for example, by centrifugation or ultrafiltration. Where the antibody is secreted into the medium, supernatants from such expression systems are generally first concentrated using a commercially available protein concentration filter, for example, an Amicon or Millipore Pellicon ultrafiltration unit. A protease inhibitor such as PMSF may be included in any of the foregoing steps to inhibit proteolysis and antibiotics may be included to prevent the growth of adventitious contaminants. [00315] The protein composition prepared from the cells can be purified using, for example, hydroxylapatite chromatography, gel electrophoresis, dialysis, and affinity chromatography, with affinity chromatography being the preferred purification technique. The matrix to which the affinity ligand is attached is most often agarose, but other matrices are available. Mechanically stable matrices such as controlled pore glass or poly (styrene-divinyl) benzene allow for faster flow rates and shorter processing times than can be achieved with agarose. Other techniques for protein purification such as fractionation on an ion-exchange column, ethanol precipitation, Reverse Phase HPLC, chromatography on silica, chromatography on heparin SEPHAROSE™ chromatography on an anion or cation exchange resin (such as a polyaspartic acid column), chromatofocusing, SDS-PAGE, and ammonium sulfate precipitation are also available depending on the antibody to be recovered. Following any preliminary purification step(s), the mixture comprising the antibody of interest and contaminants may be subjected to low pH hydrophobic interaction chromatography. Methods of Using the Antibodies [00316] In one aspect, provided herein is a method of attenuating an activity of IL-23R on a cell, comprising exposing the cell to an effective amount of an antibody or antigen binding fragment thereof provided herein. In one aspect, provided herein is a method of attenuating an activity of IL- 23R in a cell, comprising exposing the cell to an effective amount of an antibody or antigen binding fragment thereof provided herein. [00317] In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 10%. In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 20%. In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 30%. In some embodiments, the antibody provided herein attenuates an IL- 23R activity by at least about 40%. In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 50%. In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 60%. In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 70%. In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 80%. In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 90%. In some embodiments, the antibody provided herein attenuates an IL-23R activity by at least about 95%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) an IL-23R activity by at least about 15% to about 65%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) an IL-23R activity by at least about 20% to about 65%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) an IL-23R activity by at least about 30% to about 65%. [00318] A non-limiting example of an IL-23R activity is IL-23R mediated signaling. Thus, in certain embodiments, provided herein is a method of attenuating (e.g., partially attenuating) IL-23R mediated signaling in a cell, comprising exposing the cell to an effective amount of an antibody or antigen binding fragment thereof provided herein. [00319] In some embodiments, the antibody provided herein attenuates IL-23R mediated signaling by at least about 10%. In some embodiments, the antibody provided herein attenuates IL- 23R mediated signaling by at least about 20%. In some embodiments, the antibody provided herein attenuates IL-23R mediated signaling by at least about 30%. In some embodiments, the antibody provided herein attenuates IL-23R mediated signaling by at least about 40%. In some embodiments, the antibody provided herein attenuates IL-23R mediated signaling by at least about 50%. In some embodiments, the antibody provided herein attenuates IL-23R mediated signaling by at least about 60%. In some embodiments, the antibody provided herein attenuates IL-23R mediated signaling by at least about 70%. In some embodiments, the antibody provided herein attenuates IL-23R mediated signaling by at least about 80%. In some embodiments, the antibody provided herein attenuates IL- 23R mediated signaling by at least about 90%. In some embodiments, the antibody provided herein attenuates IL-23R mediated signaling by at least about 95%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) IL-23R mediated signaling by at least about 15% to about 65%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) IL-23R mediated signaling by at least about 20% to about 65%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) IL-23R mediated signaling by at least about 30% to about 65%. [00320] In some embodiments, the antibodies provided herein attenuate IL-23R binding to at least one of its ligands. [00321] Another non-limiting example of an IL-23R activity is binding to IL-23. Thus, in certain embodiments, provided herein is a method of attenuating (e.g., partially attenuating) the binding of IL-23R to IL-23, comprising exposing a cell to an effective amount of an antibody or antigen binding fragment thereof provided herein. [00322] In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 10%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 20%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 30%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 40%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 50%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 60%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 70%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 80%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 90%. In some embodiments, the antibody provided herein attenuates the binding of IL-23R to IL-23 by at least about 95%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) the binding of IL-23R to IL-23 by at least about 15% to about 65%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) the binding of IL- 23R to IL-23 by at least about 20% to about 65%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) the binding of IL-23R to IL-23 by at least about 30% to about 65%. [00323] Yet another non-limiting example of an IL-23R activity is signaling mediated by IL- 23. Thus, in certain embodiments, provided herein is a method of attenuating (e.g., partially attenuating) IL-23 mediated signaling in a cell, comprising exposing the cell to an effective amount of an antibody or antigen binding fragment thereof provided herein. [00324] In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 10%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 20%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 30%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 40%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 50%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 60%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 70%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 80%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 90%. In some embodiments, the antibody provided herein attenuates IL-23 mediated signaling by at least about 95%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) IL-23 mediated signaling by at least about 15% to about 65%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) IL-23 mediated signaling by at least about 20% to about 65%. In certain embodiments, the antibody described herein can attenuate (e.g., partially attenuate) IL-23 mediated signaling by at least about 30% to about 65%. Diagnostic Assays and Methods of Detection [00325] In one aspect, the anti-IL-23R antibodies and fragments thereof of the present disclosure are useful for detecting the presence of IL-23R in a biological sample. In an aspect, the anti-IL-23R antibodies and fragments thereof of the present disclosure are useful for detecting the presence of IL-23R on the surface of a cell or cells in a biological sample. In another aspect, the anti- IL-23R antibodies and fragments thereof of the present disclosure are useful for detecting the amount of IL-23R in a biological sample. In an aspect, the anti-IL-23R antibodies and fragments thereof of the present disclosure are useful for detecting the amount of IL-23R on the surface of a cell or cells in a biological sample. Such anti-IL-23R antibodies may include those that bind to human IL-23R but do not otherwise alter IL-23R signaling activity. The term “detecting” or “detection,” as used herein, encompasses quantitative or qualitative detection, and refers to using readouts or results of an assay to make a determination with regard to the presence/absence of IL-23R in the sample, the relative expression level IL-23R in the sample (e.g. relative to one or more reference expressions, relative to other samples, or relative to one or more expression scales), or the concentration of IL-23R in the sample. The detected readout from the assay can be numerical data, e.g. results of immunoassays, or a measured protein concentration; the detected readout can be non-numerical data, e.g. cells or tissues staining with anti-IL-23R antibodies in microscopy images or staining of IL-23R in an imaging flow cytometry; or the detected readout can be any experimental data that can be used as a proxy for the IL-23R expression as is well known to a person skilled in the art, e.g. fluorescent intensity, luminescence intensity, colorimetric readings, and absorption/emission spectroscopy. The detected readout in the assays is referred to herein as the signal of the assay. [00326] In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure bind to the native receptor on cells. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure bind to and alter the native receptor on cells. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure bind to the denatured receptor on Western blots. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to immunoprecipitate the receptor from cell lysates. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to study the cellular synthesis of the IL-23 receptor. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to study the trafficking of the IL-23 receptor. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to study the turnover of the IL-23 receptor. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to study the mechanism of action for how therapeutics affect the cellular synthesis of the IL-23 receptor. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to study the mechanism of action for how therapeutics affect the trafficking of the IL-23 receptor. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to study the mechanism of action for how therapeutics affect the turnover of the IL-23 receptor. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used in predicting drug mechanism of action and efficacious doses/exposures. In some embodiments, anti-IL- 23R antibodies and fragments thereof of the present disclosure can be used in predicting efficacious doses/exposures of therapeutics. [00327] In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on human cells. In some embodiments, anti-IL- 23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on human IL-23R transfected cell lines. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on human IL-23R transfected iLite cell lines. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on human IL-23R transfected HEK cell lines. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on primary human CD3 + CD56- T cells. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on primary human CD3 + CD56 + cells. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on primary human CD3- CD56 + cells. [00328] In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on human cells to identify IL-23-responsive cells. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on human cells to quantify IL-23-responsive cells. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on human cells to predict which diseases will respond to IL-23 pathway targeted inhibitors. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to detect the IL-23 receptor on human cells to predict which patient subsets will respond to IL-23 pathway targeted inhibitors. [00329] In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to label IL-23R-expresssing cells in healthy subjects and disease. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to sort IL-23R-expresssing cells in healthy subjects and disease. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to isolate IL-23R-expresssing cells in healthy subjects and disease. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to characterize IL-23R-expresssing cells in healthy subjects and disease. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to characterize the underlying disease pathways. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to understand mechanism of action of therapeutics. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure can be used to identify markers of response to drugs. [00330] In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure bind to the IL-23R in such a manner that they inhibit IL-23 binding and signaling. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure bind to the IL- 23R in such a manner that they compete for binding with IL-23R antagonist peptide therapeutics. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure are for use in receptor occupancy target engagement assays. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure are for use in receptor occupancy target engagement assays in blood and other tissues of patients dosed with IL-23R antagonist peptides. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure are for use in receptor occupancy target engagement assays in blood and other tissues of patients dosed with other receptor-targeted therapeutics. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure are used in target engagement assays to inform dose prediction in a range of different diseases. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure are used in target engagement assays to inform selection for future therapeutics in a range of different diseases. [00331] In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure that bind to different epitopes on IL-23R that can be used in different combinations to optimize detection of IL-23R-expressing cells. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure that bind to different epitopes on IL-23R that can be used in different combinations to optimize staining of IL-23R-expressing cells. In some embodiments, anti- IL-23R antibodies and fragments thereof of the present disclosure that bind to different epitopes on IL-23R that can be used in different combinations to optimize visualization of IL-23R-expressing cells. In some embodiments, anti-IL-23R antibodies and fragments thereof of the present disclosure that bind to different epitopes on IL-23R that can be used in different combinations to optimize quantitation of IL-23R-expressing cells. [00332] In particular embodiments, IL-23R antibodies and fragments thereof, particularly antigen-binding fragments, that bind to different epitopes on IL-23R, such as those that are set out in distinct bins, including as provided in Table 11, are used to optimize evaluation and/or quantitation of IL-23R or IL-23R-expressing cells. In an embodiment, combinations of an antibody with strong cell surface IL-23R binding and an antibody that binds to a distinct epitope, such as from a different epitope bin, that is a non-competing and also demonstrates strong cell surface IL-23R binding are provided and may be particularly preferred. [00333] In embodiments hereof, combinations of a Bin 3 antibody and a non-Bin3 antibody are contemplated and may be utilized. In embodiments hereof, combinations of a Bin 1 antibody and a non-Bin1 antibody are contemplated and may be utilized. In embodiments hereof, combinations of a Bin 5 antibody and a non-Bin5 antibody are contemplated and may be utilized. In embodiments hereof, combinations of a Bin 2 antibody and a non-Bin2 antibody are contemplated and may be utilized. In embodiments hereof, combinations of a Bin 4 antibody and a non-Bin4 antibody are contemplated and may be utilized. In embodiments hereof, combinations of a Bin 6 antibody and a non-Bin6 antibody are contemplated and may be utilized. In embodiments hereof, combinations of a Bin 7 antibody and a non-Bin7 antibody are contemplated and may be utilized. In embodiments hereof, combinations of a Bin 8 antibody and a non-Bin8 antibody are contemplated and may be utilized. In embodiments hereof, combinations of a Bin 9 antibody and a non-Bin9 antibody are contemplated and may be utilized. In embodiments, combinations of a Bin2 and a Bin 1 antibody, or of a Bin 1 and Bin5 antibody, or of a Bin 1 and Bin4 antibody, or a Bin 2 and Bin 4 antibody, or a Bin 2 and a Bin3 antibody, or a Bin 1 and Bin5 antibody, or a Bin 2 and Bin5 antibody, or a Bin3 and Bin 5 antibody, or a Bin 4 and Bin 5 antibody, or a Bin 3 and Bin 7 antibody, or a Bin1 and Bin 7 antibody, or combinations of a Bin3 antibody and a Bin 1 antibody are comtemplated and may be utilized. [00334] Bin 1 antibodies comprise antibody that binds to the same epitope and/or binds IL- 23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:202 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:203 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:252 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:253 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; or a VH comprising the amino acid sequence of SEQ ID NO:156 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:157 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. Bin 2 antibodies comprise antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:192 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:193 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:194 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:195 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:200 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:201 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:218 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:219 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:222 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:223 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:260 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:261 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:264 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:265 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:154 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:155 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:160 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:161 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; or a VH comprising the amino acid sequence of SEQ ID NO:164 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:165 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. Bin 3 antibodies comprise antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:786 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:787 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:790 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:791 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:792 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:793 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:236 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:237 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:826 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:827 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; or a VH comprising the amino acid sequence of SEQ ID NO:828 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:829 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. Bin 4 antibodies comprise antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:196 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:197 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:262 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:263 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; or a VH comprising the amino acid sequence of SEQ ID NO:152 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:153 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. Bin 5 antibodies comprise antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:798 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:799 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. Bin 6 antibodies comprise antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:206 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:207 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:250 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:251 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; a VH comprising the amino acid sequence of SEQ ID NO:144 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:145 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; or a VH comprising the amino acid sequence of SEQ ID NO:170 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:171 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. Bin 7 antibodies comprise antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:150 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:151 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. Bin 8 antibodies comprise antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:198 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:199 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; or a VH comprising the amino acid sequence of SEQ ID NO:240 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:241 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. Bin 9 antibodies comprise antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a VH comprising the amino acid sequence of SEQ ID NO:204 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:205 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof; or a VH comprising the amino acid sequence of SEQ ID NO:884 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof, and a VL comprising the amino acid sequence of SEQ ID NO:885 or comprising the CDR1, CDR2 and CDR3 domain sequences thereof. [00335] In embodiments, combinations of a Bin3 antibody and a Bin 1 antibody are comtemplated and may be utilized. In some embodiments one or more of antibody selected from I23RB1, I23RB3, I23RB4, I23RB76, I23RB269 or I23RB270, or an antibody comprising the heavy and light chain CDRs, or at least the heavy chain CDRs, of one or more of I23RB1, I23RB3, I23RB4, I23RB76, I23RB269 or I23RB270, may be combined with one or more antibody selected from I23RB42, I23RB85 or I23RB157, or an antibody comprising the heavy and light chain CDRs, or at least the heavy chain CDRs, of one or more of I23RB42, I23RB85 or I23RB157. In particular embodiments, antibody I23RB4 or I23RB76 or an antibody comprising the heavy and light chain CDRs, or at least the heavy chain CDRs, of I23RB4 or I23RB76 is combined with antibody I23RB42 or I23RB157 or an antibody comprising the heavy and light chain CDRs, or at least the heavy chain CDRs, of I23RB42 or I23RB157. [00336] In some embodiments, the affinity of the anti-IL-23R antibodies and fragments thereof of the present disclosure for human IL-23R can be determined using Surface Plasmon Resonance (SPR) methods. In some embodiments, the affinity of the anti-IL-23R antibodies and fragments thereof of the present disclosure for human IL-23R can be determined using Biolayer Interferometry (BLI) methods. In some embodiments, the affinity of the anti-IL-23R antibodies and fragments thereof of the present disclosure for human IL-23R can be determined using flow cytometry. [00337] In some embodiments, the present disclosure provides a method for detecting, selecting and/or enriching IL-23R in a sample comprising contacting the sample with the unlabeled or labeled anti-IL-23R antibodies. In certain embodiments, the method comprising using unlabeled or labeled anti-IL-23R antibodies in an IHC assay, an immunoblotting assay, a flow cytometry assay, an ELISA, a radioimmunoassay, or high throughput screening assay. [00338] In some embodiments, the present disclosure provides a method for detecting IL-23R target engagement by another therapeutic targeting IL-23R, e.g. another antibody, a peptide or a small molecule, to support dose decisions and indication decisions based on how much target engagement is achieved. [00339] In one aspect, the present disclosure provides a method of detecting the presence of IL-23R in a biological sample. In certain embodiments, the method comprises contacting the biological sample with an anti-IL-23R antibody under conditions permissive for binding of the anti- IL-23R antibody to IL-23R, and detecting the binding between an anti-IL-23R antibody and IL-23R. [00340] As provided herein, a biological sample are samples or materials that have a biological origin. Biological samples include bodily fluid, a cell or a tissue sample. In some embodiments, the cell can be a cultured cell line, engineered cells, in vitro or ex vivo culture of cells obtained from a subject, e.g. a human subject, or cells obtained from a subject. In other embodiments, the tissue samples can include bodily fluid or a tissue obtained from a subject, including a human subject. In some embodiments, the tissue samples include samples from a region of a subject suspected of having a disease. Thus tissue samples can be, but are not limited to, tissues, bodily fluid, tissue fractions, and/or cells isolated from an organism such as a mammal, in particular a human. In a particular embodiment, the tissue samples are prepared into sections that have been formalin fixed, paraffin embedded (FFPE). The cells, bodily fluid, and/or the tissue can be obtained from a subject, e.g. a human subject, by methods well known to a person skilled in the art, e.g. biopsy (including liquid biopsy), surgical procedures, cell smear, and phlebotomy. [00341] As is well known to a person skilled in the art, the amount of an antibody bound to an antigen in a biological sample correlates with the amount of the antigen in the biological sample. Therefore the amount of binding of an anti-IL-23R antibody as provided herein to IL-23R in a biological sample can be used to measure the amount or the expression level of IL-23R in the biological sample. In some embodiments, the amount of IL-23R in the biological sample is detected in the linear detection range of the anti-IL-23R antibody. The “linear detection range” refers to the range of the amount or concentration of an antigen, within which the bound antibody linearly correlates with the amount or concentration of the antigen in the biological sample. Such linear range depends on factors such as the affinity between the antibody and the antigen, the concentration of the antibody used for the antibody-antigen binding, and the condition used for the antibody-antigen binding. [00342] The concentration of the antibody used for antibody-antigen binding can be assessed in a titration experiments. In one embodiment of such titration experiments, the concentration of an antibody is serially diluted by a factor of twofold, threefold, fivefold, or tenfold, and the serially diluted antibodies were each bound to control samples with known amount of the corresponding antigen. In one embodiment, the desirable antibody concentration is that at which the amount of antibody binding differentiates the broadest linear detection range. [00343] The expression of IL-23R in a biological sample refers to the amount of IL-23R in the biological sample at a given time. The expression of IL-23R as measured reflects accumulation of IL- 23R in the biological sample over a period of time and can include degradation or modification products such as full length IL-23R, fragments of IL-23R, and naturally modified, e.g. glycosylated, IL-23R. As proteins are translated from mRNAs, the levels of mRNA in the biological samples can be used as a proxy for the expression of IL-23R in the biological samples. [00344] Provided herein are methods for assessing IL-23R expression in a tissue sample from a subject suspected of having an IL-23R-associated disease, including: (a) contacting said tissue sample with an antibody or antigen binding fragment thereof as provided herein; (b) detecting the binding of said antibody or antigen binding fragment thereof to said tissue sample; (c) determining the expression of IL-23R in the tissue sample, wherein the expression level of IL-23R in the tissue sample is compared with a reference expression level of IL-23R. [00345] Also provided herein are methods for assessing IL-23R expression in a tissue sample from a subject suspected of having an IL-23R-associated disease, including: (a) performing an IHC assay on the tissue sample with an antibody or antigen binding fragment thereof as provided herein; (b) determining the expression of IL-23R in the tissue sample, wherein the expression level of IL-23R in the tissue sample is compared with a reference expression level of IL-23R. [00346] Provided herein are also methods of assessing responsiveness of a patient to a therapeutic agent, e.g., IL-23 pathway targeted inhibitors, said method based on IL-23R expression in a tissue sample from said patient, including: (a) contacting said tissue sample with an antibody or antigen binding fragment thereof as provided herein; (b) detecting the binding of said antibody or antigen binding fragment thereof to said tissue sample; (c) determining the expression of IL-23R in the tissue sample, wherein the expression level of IL-23R in the tissue sample is compared with a reference expression level of IL-23R; wherein an increased expression level of IL-23R compared to the reference is indicative of responsiveness to said therapy. [00347] Provided herein are also methods for assessing responsiveness of patient to a therapeutic agent, e.g., IL-23 pathway targeted inhibitors, said method based on IL-23R expression in a tissue sample from said patient, including: (a) performing an IHC assay on the tissue sample with an antibody or antigen binding fragment thereof as provided herein; (b) determining the expression of IL-23R in the tissue sample, wherein the expression level of IL-23R in the tissue sample is compared with a reference expression level of IL-23R, wherein an increased expression level of IL-23R in the tissue sample compared to the reference is indicative of responsiveness to said therapy. [00348] Provided herein are methods of treating an IL-23R-associated disease in a subject including (a) determining expression level of IL-23R in a tissue sample from the subject with an antibody or antigen binding fragment thereof as provided herein, wherein the expression level of IL- 23R in the tissue sample is higher than a reference expression level of IL-23R; (b) administering a therapeutic agent to the subject. [00349] Provided herein are methods of treating an IL-23R-associated disease in a subject including (a) contacting a tissue sample from the subject with an antibody or antigen binding fragment thereof as provided herein; (b) determining expression level of IL-23R in the tissue sample from the subject with antibody or antigen binding fragment thereof as provided herein, wherein the expression level of IL-23R in the tissue sample is higher than a reference expression level of IL-23R; (c) administering a therapeutic agent to the subject. [00350] Provided herein are methods of treating an IL-23R-associated disease in a subject including (a) obtaining a tissue sample from the subject; (b) contacting the tissue sample from the subject with an antibody or antigen binding fragment thereof as provided herein; ( c) determining expression level of IL-23R in a tissue sample from the subject with an antibody or antigen binding fragment thereof as provided herein, wherein the expression level of IL-23R in the tissue sample is higher than a reference expression level of IL-23R; (d) administering a therapeutic agent to the subject. [00351] The subject in any of the method provided herein can be a human subject and the subject can have any IL-23R-associated disease for which the determination of IL-23R expression can be performed and/or for which IL-23R expression can provide diagnostic, prognostic, or predictive value. Exemplary IL-23R-associated diseases include multiple sclerosis, asthma, rheumatoid arthritis, inflammatory bowel disease (IBD), juvenile IBD, adolescent IBD, Crohn's disease, sarcoidosis, systemic elitematodes, ankylosing spondylitis, Autoimmune inflammation such as inflammation (axial spondylitic arthritis), psoriatic arthritis, or psoriasis and related diseases and disorders. In certain embodiments, the disease or disorder is psoriasis (eg, psoriasis vulgaris, guttate psoriasis), inverse psoriasis, pustular psoriasis, palmo-plantar, Psoriasis, psoriasis vulgaris, or psoriatic psoriasis, atopic dermatitis, acne ectopica, ulcerative colitis, Crohn's disease, Celiac's disease Sexual sprue, enteropathy with seronegative arthritis, microscopic colitis, collagen-accumulating colitis, eosinophilia gastroenteritis / esophagitis, colitis associated with radiation or chemotherapy, leukocyte adhesion deficiency-1 Psoriasis with congenital immunity disorders, chronic granulomatosis, glycogenosis type 1b, Hermannsky-Padrac syndrome, Chediac-East syndrome, Wiscot-Aldrich syndrome, rectal colon resection and ileal anastomosis, Later ileal psoriasis, gastrointestinal cancer, pancreatitis, insulin-dependent diabetes, mammary psoriasis, psoriasis, bile ductitis, primary biliary cirrhosis, virus-related enteropathy, periductitis, chronic bronchitis, chronic sinusitis, asthma, Psoriasis, or implant-to-host disease. Exemplary IL-23R-associated diseases include multiple sclerosis, asthma, rheumatoid arthritis, inflammation of the gut, inflammatory bowel diseases (IBDs), juvenile IBD, adolescent IBD, Crohn’s disease, ulcerative colitis, Celiac disease (nontropical Sprue), microscopic colitis, collagenous colitis, eosinophilic gastroenteritis/esophagitis, colitis associated with radio- or chemo-therapy, colitis associated with disorders of innate immunity as in leukocyte adhesion deficiency-1, sarcoidosis, Systemic Lupus Erythematosus, ankylosing spondylitis (axial spondyloarthritis), psoriatic arthritis, psoriasis (e.g., plaque psoriasis, guttate psoriasis, inverse psoriasis, pustular psoriasis, Palmo-Plantar Pustulosis, psoriasis vulgaris, or erythrodermic psoriasis), atopic dermatitis, acne ectopica, enteropathy associated with seronegative arthropathies, chronic granulomatous disease, glycogen storage disease type 1b, Hermansky-Pudlak syndrome, Chediak-Higashi syndrome, Wiskott-Aldrich Syndrome, pouchitis, pouchitis resulting after proctocolectomy and ileoanal anastomosis, gastrointestinal cancer, pancreatitis, insulin-dependent diabetes mellitus, mastitis, cholecystitis, cholangitis, primary biliary cirrhosis, viral-associated enteropathy, pericholangitis, chronic bronchitis, chronic sinusitis, asthma, uveitis, or graft versus host disease. In some embodiments, the IL-23R-associated diseases are specifically selected from subset of inflammatory diseases, which include, but are not limited to psoriasis (PSO), psoriatic arthritis (PSA), inflammatory bowel disease (IBD), Crohn's disease (CD), or ulcerative colitis (UC). The disease or disorder may be an autoimmune disease. In some embodiments, the automimmine disease is selected from Ulcerative colitis (UC), Crohn’s Disease (CD), psoriasis (PsO), or psoriatic arthritis (PsA). [00352] As used herein, the term “responsiveness” refers to the probability of a cell or an individual or a patient or a subject responding or having a reaction to the treatment of a therapeutic agent. The responsiveness can include the probability of a wide range of reactions to the therapeutic agent, for example and without any limitation, (i) reduce or ameliorate the severity of the disease, disorder or condition to be treated or a symptom associated therewith; (ii) reduce the duration of the disease, disorder or condition to be treated, or a symptom associated therewith; (iii) prevent the progression of the disease, disorder or condition to be treated, or a symptom associated therewith; (iv) cause regression of the disease, disorder or condition to be treated, or a symptom associated therewith; (v) prevent the development or onset of the disease, disorder or condition to be treated, or a symptom associated therewith; (vi) prevent the recurrence of the disease, disorder or condition to be treated, or a symptom associated therewith; (vii) reduce hospitalization of a subject having the disease, disorder or condition to be treated, or a symptom associated therewith; (viii) reduce hospitalization length of a subject having the disease, disorder or condition to be treated, or a symptom associated therewith; (ix) increase the survival of a subject with the disease, disorder or condition to be treated, or a symptom associated therewith; (xi) inhibit or reduce the disease, disorder or condition to be treated, or a symptom associated therewith in a subject; and/or (xii) enhance or improve the prophylactic or therapeutic effect(s) of another therapy. In certain embodiments, the cell or tissue or individual or patient or subject is more likely to respond to a therapeutic agent, e.g., IL-23 pathway targeted inhibitors, when the cell, tissue, patient, or subject shows a significant expression IL-23R in its cells. In certain embodiments, the responsiveness increases with the increased level of IL-23R in cells. In certain embodiments, the responsiveness correlates with the level of IL-23R expression in cells. In certain embodiments, the responsiveness is linearly proportional to the level of IL-23R expression in cells. In other embodiments, the responsiveness of a cell, tissue, patient, or subject to a therapeutic agent can be 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 120%, 150%, 200%, 250%, 300%, 400%, 500%, 750%, 10 times, 15 times, 20 times, 30 times, 40 times, 50 times, 60 times, 70 times, 80 times, 90 times, 100 times, or more than the cells negative for IL-23R expression. [00353] As used herein, “indicative of responsiveness” refers to a prediction that the responsiveness will be higher in one cell, tissue, human individual, or subject, over another cell, tissue, human individual, or subject. Such predictions are made based on certain criteria. In some embodiments, the prediction of the responsiveness is made based on the expression level of IL-23R in the cell, tissue, human individual, or subject. As described above, in certain embodiments, the cell or tissue or individual or patient or subject is predicted to be more likely to respond to a therapeutic agent, e.g., IL-23 pathway targeted inhibitors, when the cell, tissue, patient, or subject shows a significant expression of IL-23R in its cells. In certain embodiments, the responsiveness is predicted to increase with the increased level of IL-23R in its cells. In certain embodiments, the responsiveness is predicted to correlate with the level of IL-23R in its cells. In certain embodiments, the responsiveness is predicted to be linearly proportional to the level of IL-23R in its cells. In other embodiments, the responsiveness of a cell, tissue, patient, or subject to a therapeutic agent, e.g., IL- 23 pathway targeted inhibitors, is predicted to be 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 120%, 150%, 200%, 250%, 300%, 400%, 500%, 750%, 10 times, 15 times, 20 times, 30 times, 40 times, 50 times, 60 times, 70 times, 80 times, 90 times, 100 times, or more than the cells negative for IL-23R expression. [00354] The therapeutic agent can be any disease therapy for which IL-23R expression can provide diagnostic, prognostic, or predictive value. In certain embodiments, the therapeutic agent is one that targets biological processes, e.g. a signaling pathway, a metabolic pathway, or a protein synthesis/degradation pathway, in which IL-23R plays a role. In certain embodiments, the therapeutic agent is one that targets IL-23R activity, IL-23R signaling, or IL-23R mediated diseases. In a specific embodiment, the therapeutic agent is an anti-IL-23R antibody or an anti-IL-23R antibody drug conjugate. [00355] For determining the expression of IL-23R in the tissue sample, the expression level of IL-23R in the tissue sample is compared or correlated with a reference expression level of IL-23R. The “reference expression level” as used herein refers to an expression level in a reference sample that, when compared with the IL-23R expression level in the test sample, provides relative information about IL-23R expression in the test sample. The reference expression level can be a known expression level, e.g. expression in a reference sample where the amount, concentration, and/or mole quantity of IL-23R is known. For example, the reference expression level can be the IL- 23R expression in a cell line where the cells have been transfected or otherwise engineered to express a known amount of IL-23R. In some embodiments, reference expression level can be the IL-23R expression in a cell where the IL-23R expression has been quantitated by methods provided herein or known to a person skilled in the art, such as ELISA, SDS-PAGE, quantitative immunoprecipitation, and /or quantitative western blotting. In other embodiments, reference expression level involves more than one reference, such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 14, 16, 18, 20, 25, 30, 35, 40, 45, 50, 75, 100, and more references. In one embodiment, the reference level has 4 references: one negative for IL- 23R expression, one with weak IL-23R expression, one with moderate IL-23R expression, and one with high/strong IL-23R expression. [00356] Alternatively, a reference expression level can be a level where the exact concentration or quantity of IL-23R is unknown but the status, activity, and/or function of the reference sample is known. In some embodiments, the reference expression levels can be those of a non-diseased cell from the same patient that is suspected of having IL-23R-associated disease. In such embodiments, by comparing IL-23R expression in the test sample with that in the reference sample, the IL-23R expression in the test sample relative to (e.g. higher than, lower than, or substantially the same as) the IL-23R expression of the non-diseased cells can be determined. In other embodiments, the reference expression levels can be those of diseased cells, wherein by comparing IL-23R expression in the test sample with that in the reference sample, the IL-23R expression in the test sample relative to (e.g. higher than, lower than, or substantially the same as) the IL-23R expression of the diseased cells can be determined. In other embodiments, the reference expression levels can be those of a cell from a second subject, wherein by comparing IL-23R expression in the test sample with that in the reference sample, the IL-23R expression in the test sample relative to (e.g. higher than, lower than, or substantially the same as) the IL-23R expression of the cells from a second subject can be determined. The second subject can be a normal human subject having no IL-23R- associated disease, a human subject having the same kind of IL-23R-associated disease as that the patient is suspected of having, or a human subject having a different kind of IL-23R-associated disease from what the patient is suspected of having. [00357] The reference sample and reference cells as described herein can be a cell line, in vitro or ex vivo culture of cells obtained from patient suspected of having IL-23R-associated disease, cells obtained from patient suspected of having IL-23R-associated disease, in vitro or ex vivo culture of cells obtained from a second subject, cells obtained from a second subject. [00358] Therefore, in some embodiments of the methods provided herein, the reference expression level of IL-23R can be the IL-23R expression level in IL-23R-associated diseased cells, non-diseased cells of said subject, or non-diseased cells from a second subject. [00359] As described above, in some embodiments, the IL-23R expression in a sample can be determined by correlating or comparing the anti-IL-23R antibody binding to the sample with the anti- IL-23R antibody binding to the negative and positive references, wherein the levels of IL-23R expression in the references are known. The reference IL-23R expression can be a positive IL-23R control or a negative IL-23R control. As used herein, a “positive IL-23R control” or a “positive control” refers to a cell, a tissue, a tumor, a human, and/or a subject known to express significant amount of IL-23R. A “negative IL-23R control” or “negative control” refers to cells and/or tissues known to express no IL-23R or low level of IL-23R such that the IL-23R in the cells or tissues are not biologically significant. IL-23R level is biologically insignificant when (1) a person skilled in the art would consider the level of IL-23R expression low in light of a protein product of a house keeping gene; (2) the presence or absence of the low amount of IL-23R does not make a biological difference to the cell or tissue; and (3) if these insignificant amount of IL-23R is removed or deleted from the cells or tissues, the cells or tissues will continue to function substantially the same way as before such removal or deletion. The known IL23R gene expression but not protein expression can be determined independently by a qPCR assay. The known IL-23R protein expression can also be independently determined using any below described immunoassays with an anti-IL-23R antibody that has been determined to be IL-23R specific, (e.g. an IL-23R specific antibody identified in the specificity- screening methods described above). Suitable immunoassays include, by way of example and without any limitation, an IHC assay, an immunoblotting assay, a FACS assay, or an ELISA. In some embodiments, the IL23R mRNA level may not be zero in the negative control due to the background noise of the assays or due to the biologically insignificant low level of remaining IL-23R. Negative IL-23R control can be properly considered negative for IL-23R, for example, when the IL23R mRNA level in a qPCR assay is substantially similar to the level of mRNA detected with a set of nonspecific primers, or when the IL23R mRNA level is biologically insignificant in light of the IL23R mRNA level in a positive IL-23R control. Similarly, the IL-23R detected by immunoassays using another IL- 23R specific antibody in a negative control may not be zero due to background noise of the assays or due to the biologically insignificant low level of remaining IL-23R. The background noise can be caused by non-specific interactions between the assay reagents other than the anti-IL-23R antibodies and the samples. The negative IL-23R control can be properly considered negative for IL-23R, for example, when the IL-23R level in the negative control detected by the anti-IL-23R antibody is substantially similar to the detection level from an isotype control antibody in the same assay. In some assays, the background noise can account for a substantial percentage of the detected signal from the IL-23R expression. [00360] Additionally, positive and negative controls have been identified and published in the literature by persons skilled in the art, including positive and/or negative tissues, cells (including, e.g. cell lines), and pathological samples. Such literature can be readily identified by searching databases such as PubMed (e.g. using search terms such as IL-23R, expression, positive, negative, and/or distribution) and analyzing the search hits. [00361] Accordingly, the relative amount of the antibody or antigen-binding fragment thereof bound to a negative control cell with no IL-23R expression can be about 50%, 40%, 30%, 20%, 10%, 5%, 4%, 3%, 2%, 1% , 0.5%, 0.3%, 0.2%, 0.1%, 0.05%, 0.03%, 0.01%, 0.001% or less of the amount of the antibody or antigen-binding fragment thereof bound to the sample cell expressing IL-23R. [00362] Therefore, in some embodiments of the methods provided herein, the reference expression level of IL-23R is the IL-23R expression level in a negative control, wherein the IL-23R expression in the negative control is independently determined by a qPCR assay, an IHC assay with a second antibody, an immunoblotting assay with a second antibody, a FACS assay with a second antibody, or an ELISA with a second antibody. [00363] In other embodiments of the methods provided herein, the reference expression level of IL-23R is the IL-23R expression level in a positive control cell expressing IL-23R, wherein the IL- 23R expression in the positive control is independently determined by a qPCR assay, an IHC assay with a second antibody, an immunoblotting assay with a second antibody, a FACS assay with a second antibody, or an ELISA with a second antibody. [00364] The expression level of IL-23R in a sample can be different from that in a positive control. The relative amount of the antibody or antigen-binding fragment thereof bound to the tissue sample can be about 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 120%, 150%, 200%, 250%, 300% , 400%, 500%, 750%, 10 times, 15 times, 20 times, 30 times, 40 times, 50 times, 60 times, 70 times, 80 times, 90 times, 100 times, 200 times, 500 times, or more of the amount of the antibody or antigen-binding fragment thereof bound to the positive control cell expressing IL-23R. [00365] Numerous different PCR or qPCR protocols are known in the art and exemplified herein below and can be directly applied or adapted for determining the IL23R mRNA level in the samples or controls, which can be used as a proxy for the expression levels of IL-23R protein in the samples or controls. Quantitative PCR (qPCR) (also referred as real-time PCR) is applied and adapted in some embodiments as it provides not only a quantitative measurement, but also reduced time and contamination. As used herein, “quantitative PCR (or “qPCR”) refers to the direct monitoring of the progress of PCR amplification as it is occurring without the need for repeated sampling of the reaction products. In quantitative PCR, the reaction products can be monitored via a signaling mechanism (e.g., fluorescence) as they are generated and are tracked after the signal rises above a background level but before the reaction reaches a plateau. The number of cycles required to achieve a detectable or “threshold” level of fluorescence varies directly with the concentration of amplifiable targets at the beginning of the PCR process, enabling a measure of signal intensity to provide a measure of the amount of target nucleic acid in a sample in real time. When qPCR is applied to determine mRNA expression level, an extra step of reverse-transcription of mRNA to DNA is performed before the qPCR analysis. Examples of PCR methods can be found in the literature (Wong et al., BioTechniques 39:75-85 (2005); D’haene et al., Methods 50:262–270 (2010)), which is incorporated by reference herein in its entirety. Examples of PCR assays can be found in U.S. Patent No.6,927,024, which is incorporated by reference herein in its entirety. Examples of RT-PCR methods can be found in U.S. Patent No.7,122,799, which is incorporated by reference herein in its entirety. A method of fluorescent in situ PCR is described in U.S. Patent No.7,186,507, which is incorporated by reference herein in its entirety. [00366] In one specific embodiment, qPCR can be performed to determine or measure the IL23R mRNA levels as follows. Briefly, mean Ct (cycle threshold) values (or referred to herein interchangeably as Cq (quantification cycle)) of replicate qPCR reactions for IL23R and one or more housekeeping genes are determined. Mean Ct values for IL23R can be then normalized to the Ct values of the housekeeping genes using the following exemplary formula: IL23R-∆Ct = (mean Ct of IL23R –mean Ct of housekeeping gene A). The relative IL23R-∆Ct can then be used to determine relative level of IL23R mRNA, for example by using the formula of mRNA expression = 2 –∆Ct . For a summary of Ct and Cq values, see MIQE guideline (Bustin et al., The MIQE Guidelines: Minimum Information for Publication of Quantitative Real-Time PCR Experiments, Clinical Chemistry 55:4 (2009)). [00367] Other commonly used methods known in the art for the quantification of mRNA expression in a sample can also be used, including northern blotting and in situ hybridization (Parker & Barnes, Methods in Molecular Biology 106:247-283 (1999)); RNAse protection assays (Hod, Biotechniques 13:852- 854 (1992)); microarrays (Hoheisel et al., Nature Reviews Genetics 7:200-210 (2006); Jaluria et al., Microbial Cell Factories 6:4 (2007)); and polymerase chain reaction (PCR) (Weis et al, Trends in Genetics 8:263-264 (1992)). Alternatively, levels of mRNA expression can be determined by sequencing techniques. Representative methods for sequencing-based gene expression analysis include Serial Analysis of Gene Expression (SAGE), and gene expression analysis by massively parallel signature sequencing (MPSS). [00368] As described earlier, tissue samples can be, but are not limited to, tissues, bodily fluid, tissue fractions, and/or cells isolated from an organism such as a mammal, in particular a human. Therefore, tissue samples can be obtained from a variety of organs of a subject, including a human subject. In some embodiments, tissue samples are obtained from organs suspected of having a disease, dysfunction or disorder, such as an immune disease. In other embodiments, tissue samples are obtained from normal organs from the patient who is being tested or from a second human subject. [00369] Anti-IL-23R antibodies bound to the samples can be detected by a variety of immunoassays known in the art, including an IHC approach, an immunoblotting assay, a FACS assay, and an ELISA. [00370] IL-23R can be detected by an anti-IL-23R antibody in a variety of IHC approaches. IHC staining of tissue sections has been shown to be a reliable method of assessing or detecting the presence of proteins in a sample. IHC techniques utilize an antibody to probe and visualize cellular antigens in situ, generally by chromogenic or fluorescent methods. Primary antibodies or antisera, such as polyclonal antisera and monoclonal antibodies that specifically target IL-23R, can be used to detect expression in an IHC assay. In some embodiments, the tissue sample is contacted with a primary antibody for a specific target for a period of time sufficient for the antibody-target binding to occur. As discussed in detail earlier, the antibodies can be detected by direct labels on the antibodies themselves, for example, radioactive labels, fluorescent labels, hapten labels such as biotin, or an enzyme such as horse radish peroxidase or alkaline phosphatase. Alternatively, unlabeled primary antibody is used in conjunction with a labeled secondary antibody, comprising antisera, polyclonal antisera or a monoclonal antibody specific for the primary antibody. IHC protocols and kits are well known in the art and are commercially available. Automated systems for slide preparation and IHC processing are available commercially. The Leica BOND Autostainer and Leica Bond Refine Detection system is an example of such an automated system. [00371] In some embodiments, an IHC assay is performed with an unlabeled primary antibody in conjunction with a labeled secondary antibody in an indirect assay. The indirect assay utilizes two antibodies for the detection of target proteins such as IL-23R in a tissue sample. First, an unconjugated primary antibody was applied to the tissue (first layer), which reacts with the target antigen in the tissue sample. Next, an enzyme-labeled secondary antibody is applied, which specifically recognizes the antibody isotype of the primary antibody (second layer). The secondary antibody reacts with the primary antibody, followed by substrate-chromogen application. The second-layer antibody can be labeled with an enzyme such as a peroxidase, which reacts with the chromogen 3, 3’-diaminobenzidine (DAB) to produce brown precipitate at the reaction site. This method is sensitive and versatile due to the potential signal amplification through a signal amplification system. [00372] In certain embodiments to increase the sensitivity of the detection, a signal amplification system can be used. “A signal amplification system”, as used herein, means a system of reagents and methods that can be used to increase the signal from detecting the bound primary or the secondary antibody. A signal amplification system increases the sensitivity of the target protein detection, increases the detected signal, and decreases the lower boundary of the detection limits. There are several types of signal amplification systems including an enzyme labeling system and macrolabeling system. These systems/approaches are not mutually exclusive and can be used in combination for additive effect. [00373] Macrolabels or macrolabeling system are collections of labels numbering in the tens (e.g. phycobiliproteins) to millions (e.g. fluorescent microspheres) attached to or incorporated in a common scaffold. The scaffold can be coupled to a target-specific affinity reagent such as an antibody, and the incorporated labels are thereby collectively associated with the target upon binding. The labels in the macrolabels can be any of the labels described herein such as fluorophores, haptens, enzymes, and/or radioisotopes. In one embodiment of the signal amplification system, a labeled chain polymer-conjugated secondary antibody was used. The polymer technology utilized an HRP enzyme- labeled inert “spine” molecule of dextran to which 1, 2, 3, 4, 5, 6, 7, 8, 910, 15, 20, 25, 30, 50 or more molecules of secondary antibodies can be attached, making the system even more sensitive. [00374] Signal amplification system based on an enzyme labeling system utilizes the catalytic activity of enzymes, such as horseradish peroxidase (HRP) or alkaline phosphatase to generate high- density labeling of a target protein or nucleic acid sequence in situ. In one embodiment, tyramide can be used to increase the signal of HRP. In such a system, HRP enzymatically converts the labeled tyramide derivative into highly reactive, short-lived tyramide radicals. The labeled active tyramide radicals then covalently couple to residues (principally the phenol moiety of protein tyrosine residues) in the vicinity of the HRP-antibody–target interaction site, resulting in amplification of the number of labels at the site with minimal diffusion-related loss of signal localization. Consequently, the signal can be amplified 1, 2, 3, 4, 5, 6, 7, 8, 910, 15, 20, 25, 30, 50, 75, or 100 folds. As known to a person skilled in the art, the labels on the tyramide can be any labels described herein, including fluorophores, enzymes, haptens, radioisotopes, and/or photophores. Other enzyme-based reactions can be utilized to create signal amplification as well. For example, Enzyme-Labeled Fluorescence (ELF) signal amplification is available for alkaline phosphatase, wherein the alkaline phosphatase enzymatically cleaves a weakly blue-fluorescent substrate (ELF 97 phosphate) and converts it into a bright yellow-green-fluorescent precipitate that exhibits an unusually large Stokes shift and excellent photostability. Both tyramide-based signal amplification system and ELF signal amplification are available commercially, for example from ThermoFisher Scientific (Waltham, MA USA 02451). [00375] Thus in some embodiments of the methods provided herein, the expression level of IL-23R is detected with a signal amplification system. [00376] In some embodiments, the specimen is then counterstained to identify cellular and subcellular elements. [00377] In some embodiments, the expression level of IL-23R can also be detected with antibodies described herein using an immunoblotting assay. In some embodiments of an immunoblotting assay proteins are often (but do not have to be) separated by electrophoresis and transferred onto membranes (usually nitrocellulose or PVDF membrane). Similar to the IHC assays, primary antibodies or antisera, such as polyclonal antisera and monoclonal antibodies that specifically target IL-23R, can be used to detect protein expression. In some embodiments, the membrane is contacted with a primary antibody for a specific target for a period of time sufficient for the antibody- antigen binding to occur and the bound antibodies can be detected by direct labels on the primary antibodies themselves, e.g. with radioactive labels, fluorescent labels, hapten labels such as biotin, or enzymes such as horseradish peroxidase or alkaline phosphatase. In other embodiments, unlabeled primary antibody is used in an indirect assay as described above in conjunction with a labeled secondary antibody specific for the primary antibody. As described herein, the secondary antibodies can be labeled, for example, with enzymes or other detectable labels such as fluorescent labels, luminescent labels, colorimetric labels, or radioisotopes. Immunoblotting protocols and kits are well known in the art and are commercially available. Automated systems for immunoblotting, e.g. iBind Western Systems for Western blotting (ThermoFisher, Waltham, MA USA 02451), are available commercially. Immunoblotting includes, but is not limited to, Western blot, in-cell Western blot, and dot blot. Dot blot is a simplified procedure in which protein samples are not separated by electrophoresis but are spotted directly onto a membrane. In cell Western blot involves seeding cells in microtiter plates, fixing/permeabilizing the cells, and subsequent detection with a primary labeled primary antibody or unlabeled primary antibody followed by labeled secondary antibody as described herein. [00378] In other embodiments, the expression levels of IL-23R can also be detected with the antibodies described herein in a flow cytometry assay, including a fluorescence-activated cell sorting (FACS) assay. Similar to the IHC or immunoblotting assays, primary antibodies or antisera, such as polyclonal antisera and monoclonal antibodies that specifically target IL-23R, can be used to detect protein expression in a FACS assay. In some embodiments, cells are stained with primary antibodies against specific target protein for a period of time sufficient for the antibody-antigen binding to occur and the bound antibodies can be detected by direct labels on the primary antibodies, for example, fluorescent labels or hapten labels such as biotin on the primary antibodies. In other embodiments, unlabeled primary antibody is used in an indirect assay as described above in conjunction with a fluorescently labeled secondary antibody specific for the primary antibody. FACS provides a method for sorting or analyzing a mixture of fluorescently labeled biological cells, one cell at a time, based upon the specific light scattering and fluorescent characteristics of each cell. The flow cytometer thus detects and reports the intensity of the fluorchrome-tagged antibody, which indicates the expression level of the target protein. Therefore, the expression level of surface proteins (such as IL-23R) can be detected using antibodies against the target protein. Non-fluorescent cytoplasmic proteins can also be observed by staining permeablized cells. Methods for performing FACS staining and analyses are well known to a person skilled in the art and are described by Teresa S. Hawley and Robert G. Hawley in Flow Cytometry Protocols, Humana Press, 2011 (ISBN 1617379506, 9781617379505). [00379] In other embodiments, the expression levels of IL-23R can also be detected using immunoassays such as an Enzyme Immune Assay (EIA) or an ELISA. Both EIA and ELISA assays are known in the art, e.g. for assaying a wide variety of tissues and samples, including blood, plasma, serum or bone marrow. A wide range of ELISA assay formats are available, see, e.g., U.S. Pat. Nos. 4,016,043, 4,424,279, and 4,018,653, which are hereby incorporated by reference in their entireties. These include both single-site and two-site or “sandwich” assays of the non-competitive types, as well as in the traditional competitive binding assays. These assays also include direct binding of a labeled antibody to a target protein. Sandwich assays are commonly used assays. A number of variations of the sandwich assay technique exist. For example, in a typical forward assay, an unlabeled antibody is immobilized on a solid substrate, and the sample to be tested brought into contact with the bound molecule. After a suitable period of incubation, for a period of time sufficient to allow formation of an antibody-antigen complex, a second antibody specific to the antigen, labeled with a reporter molecule capable of producing a detectable signal is then added and incubated, allowing time sufficient for the formation of another complex of antibody-antigen-labeled antibody. Any unreacted material is washed away, and the presence of the antigen is determined by observation of a signal produced by the reporter molecule. The results may either be qualitative, by simple observation of the visible signal, or may be quantitated by comparing with a control sample containing known amounts of target protein. [00380] In some embodiments of the EIA or ELISA assays, an enzyme is conjugated to the second antibody. In other embodiments, fluorescently labeled secondary antibodies can be used in lieu of the enzyme-labeled secondary antibody to produce a detectable signal in ELISA assay format. When activated by illumination with light of a particular wavelength, the fluorochrome-labeled antibody adsorbs the light energy, inducing a state to excitability in the molecule, followed by emission of the light at a characteristic color visually detectable with a light microscope. As in the EIA and ELISA, the fluorescent labeled antibody is allowed to bind to the first antibody-target protein complex. After washing off the unbound reagent, the remaining tertiary complex is then exposed to the light of the appropriate wavelength, the fluorescence observed indicates the presence of the target protein of interest. Immunofluorescence and EIA techniques are both very well established in the art and are disclosed herein. [00381] For the immunoassays described herein, any of a number of enzymes or non-enzyme labels can be utilized so long as the enzymatic activity or non-enzyme label, respectively, can be detected. The enzyme thereby produces a detectable signal, which can be utilized to detect a target protein. Particularly useful detectable signals are chromogenic or fluorogenic signals. Accordingly, particularly useful enzymes for use as a label include those for which a chromogenic or fluorogenic substrate is available. Such chromogenic or fluorogenic substrates can be converted by enzymatic reaction to a readily detectable chromogenic or fluorescent product, which can be readily detected and/or quantified using microscopy or spectroscopy. Such enzymes are well known to those skilled in the art, including but not limited to, horseradish peroxidase, alkaline phosphatase, ^-galactosidase, glucose oxidase, and the like (see Hermanson, Bioconjugate Techniques, Academic Press, San Diego (1996)). Other enzymes that have well known chromogenic or fluorogenic substrates include various peptidases, where chromogenic or fluorogenic peptide substrates can be utilized to detect proteolytic cleavage reactions. The use of chromogenic and fluorogenic substrates is also well known in bacterial diagnostics, including but not limited to the use of ^- and ^-galactosidase, ^-glucuronidase,6- phospho- ^-D-galatoside 6-phosphogalactohydrolase, ^-gluosidase, ^-glucosidase, amylase, neuraminidase, esterases, lipases, and the like (Manafi et al., Microbiol. Rev.55:335-348 (1991)), and such enzymes with known chromogenic or fluorogenic substrates can readily be adapted for use in methods of the present invention. [00382] Various chromogenic or fluorogenic substrates to produce detectable signals are well known to those skilled in the art and are commercially available. Exemplary substrates that can be utilized to produce a detectable signal include, but are not limited to, 3,3'-diaminobenzidine (DAB), 3,3’,5,5’-tetramethylbenzidine (TMB), Chloronaphthol (4-CN)(4-chloro-1-naphthol), 2,2'-azino-bis(3- ethylbenzothiazoline-6-sulphonic acid) (ABTS), o-phenylenediamine dihydrochloride (OPD), and 3- amino-9-ethylcarbazole (AEC) for horseradish peroxidase; 5-bromo-4-chloro-3-indolyl-1-phosphate (BCIP), nitroblue tetrazolium (NBT), Fast Red (Fast Red TR/AS-MX), and p-Nitrophenyl Phosphate (PNPP) for alkaline phosphatase; 1-Methyl-3-indolyl-β-D-galactopyranoside and 2-Methoxy-4-(2- nitrovinyl)phenyl β-D-galactopyranoside for ^-galactosidase; 2-Methoxy-4-(2-nitrovinyl)phenyl β-D- glucopyranoside for ^-glucosidase; and the like. Exemplary fluorogenic substrates include, but are not limited to, 4-(Trifluoromethyl)umbelliferyl phosphate for alkaline phosphatase; 4- Methylumbelliferyl phosphate bis (2-amino- 2-methyl-1,3-propanediol), 4-Methylumbelliferyl phosphate bis (cyclohexylammonium) and 4-Methylumbelliferyl phosphate for phosphatases; QuantaBlu TM and QuantaRed TM for horseradish peroxidase; 4-Methylumbelliferyl β-D- galactopyranoside, Fluorescein di(β-D-galactopyranoside) and Naphthofluorescein di-(β-D- galactopyranoside) for β-galactosidase; 3-Acetylumbelliferyl β-D-glucopyranoside and 4- Methylumbelliferyl-β- D-glucopyranoside for β-glucosidase; and 4-Methylumbelliferyl-α- D- galactopyranoside for α-galactosidase. Exemplary enzymes and substrates for producing a detectable signal are also described, for example, in US publication 2012/0100540. Various detectable enzyme substrates, including chromogenic or fluorogenic substrates, are well known and commercially available (Pierce, Rockford IL; Santa Cruz Biotechnology, Dallas TX; Invitrogen, Carlsbad CA; 42 Life Science; Biocare). Generally, the substrates are converted to products that form precipitates that are deposited at the site of the target nucleic acid. Other exemplary substrates include, but are not limited to, HRP-Green (42 Life Science), Betazoid DAB, Cardassian DAB, Romulin AEC, Bajoran Purple, Vina Green, Deep Space Black™, Warp Red™, Vulcan Fast Red and Ferangi Blue from Biocare (Concord CA; biocare.net/products/detection/chromogens). [00383] In some embodiments of the immunoassays, a detectable label can be directly coupled to either the primary antibody or the secondary antibody that detects the unlabeled primary antibody can have. Exemplary detectable labels are well known to those skilled in the art, including but not limited to chromogenic or fluorescent labels (see Hermanson, Bioconjugate Techniques, Academic Press, San Diego (1996)). Exemplary fluorophores useful as labels include, but are not limited to, rhodamine derivatives, for example, tetramethylrhodamine, rhodamine B, rhodamine 6G, sulforhodamine B, Texas Red (sulforhodamine 101), rhodamine 110, and derivatives thereof such as tetramethylrhodamine-5-(or 6), lissamine rhodamine B, and the like; 7-nitrobenz-2-oxa-1,3-diazole (NBD); fluorescein and derivatives thereof; napthalenes such as dansyl (5-dimethylaminonapthalene- 1-sulfonyl); coumarin derivatives such as 7-amino-4-methylcoumarin-3-acetic acid (AMCA), 7- diethylamino-3-[(4'-(iodoacetyl)amino)phenyl]-4-methylcoumar in (DCIA), Alexa fluor dyes (Molecular Probes), and the like; 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene (BODIPY TM ) and derivatives thereof (Molecular Probes; Eugene Oreg.); pyrenes and sulfonated pyrenes such as Cascade Blue TM and derivatives thereof, including 8-methoxypyrene-1,3,6-trisulfonic acid, and the like; pyridyloxazole derivatives and dapoxyl derivatives (Molecular Probes); Lucifer Yellow (3,6- disulfonate-4-amino-naphthalimide) and derivatives thereof; CyDye TM fluorescent dyes (Amersham/GE Healthcare Life Sciences; Piscataway NJ), and the like. Exemplary chromophores include, but are not limited to, phenolphthalein, malachite green, nitroaromatics such as nitrophenyl, diazo dyes, dabsyl (4-dimethylaminoazobenzene-4'-sulfonyl), and the like. [00384] Methods well known to a person skilled in the art such as microscopy or spectroscopy can be utilized to visualize chromogenic or fluorescent detectable signals associated with the bound primary or secondary antibodies. [00385] “Determining the expression of IL-23R” refers to putting the expression of IL-23R in the test biological sample in a referenced system (or a referenced scale) so that a person familiar with the referenced system can tell the relative expression of IL-23R in the test sample with respect to other samples that have been positioned in the referenced system. Consequently, such a determination involves comparing the expression of IL-23R in the test tissue sample with a reference expression level of IL-23R. [00386] In some embodiments, the referenced system can be a quantitative system where the actual molar concentration or mole quantity of IL-23R in the test sample is compared with the molar concentration or mole quantity of the reference expression levels. In some embodiments, other surrogate numerical measurements that are linearly proportional to the molar concentration or mole quantity can be used. Examples of these surrogate measurements include fluorescence intensity measurements of bound antibodies, luminescence intensity measurements of bound antibodies, radioactivity measurements of bound antibodies, and/or colorimetric or chromogenic measurements of bound antibodies. [00387] In other embodiments, the referenced system can be a categorization system. A categorization system can have as few as 2 categories and as many as 3, 4, 5, 6, 7, 8, 9, 10, 12, 14, 16, 18, 20, 25, 30, 35, 40, 45, 50, 75, 100, or more categories. In one embodiment, the referenced system has a positive category for samples that are positive for IL-23R expression (positive) and a negative category for samples that are negative for IL-23R expression (negative). In such a categorization system, determining the expression of IL-23R in a test sample involves comparing the expression of IL-23R in the test sample with IL-23R expression of a positive reference sample and/or with a negative reference, and placing the test sample in the positive category if the test sample expresses IL- 23R at a similar or higher level than the positive reference. In another embodiment, the categorization system has 3 categories, e.g. negative, medium, and high expression categories. In another embodiment, the categorization system has 4 categories, e.g. negative, low/weak, medium/moderate, and high/strong expression categories. In some aspects, determining the expression of IL-23R in a test sample involves comparing the expression of IL-23R in the test sample with one or more references of IL-23R expression of known categories and placing the test sample in a category according to its relative expression to the reference(s). [00388] In some embodiments, the referenced system can be a scoring system. A scoring system can be similar to a categorization system except that the categories are replaced by a score. For example, a 2-category system of negative and positive IL-23R expression can be a scoring system of 0 and 1, where 0 means negative and 1 means positive. In another embodiment, a 3-category system can be a scoring system of 0, 1, and 2, wherein 0 is negative, 1 is low/weak expression, and 2 is medium/moderate and high/strong expression. In another embodiment, a 4-category system can be a scoring system of 0, 1, 2, and 3, where in 0 is negative, 1 is low/weak, 2 is medium/moderate, and 3 is high/strong expression. Similar to the categorization system, determining the expression of IL-23R in a test sample in the scoring system involves comparing the expression of IL-23R in the test sample with one or more references of IL-23R expression having a known score and assigning the test sample a score according to its relative expression to the references. The scoring system, however, can be scores of discontinuous and discrete numbers (e.g. a system of 0, 2, 4, 6, 8, and 10, or a system of 1, 4, 6, 11, 13, and 19), numbers with fractions (e.g.1, 1.5, 2, 2.5, 3, 3.5 etc), negative numbers, numbers starting from any number (e.g.1000, 2000, 3000, etc), and any set of numbers that can be used to track the relative protein expression in biological samples. [00389] In some embodiments, the referenced system can be percentages of cells in conjunction with the categorization or scoring systems. The combination of percentage of cells with a categorization or scoring system provides finer gradation of the samples. In such a combined system, each cell from the biological sample is assigned or placed in the categorization or scoring system, and the approximate percentage of cells of the test sample in each category or score is determined. In one example, measurements of percentages of cells can be coupled with a 2-category system of positive and negative IL-23R expression, wherein the sample is not measured as a whole but break into the percentage of cells that are positive for IL-23R expression and percentage of cells that are negative for IL-23R expression. For example, in a 2-category system of positive and negative IL-23R expression, a test sample may be negative for IL-23R expression if placed in a 2 category system but have 10% cells positive for IL-23R expression and 90% of cells negative for IL-23R expression. In one embodiment, the referenced system includes percentages of cells in conjunction with a 2-category or 2-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with a 3-category or 3-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with a 4-category or 4-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with a 5-category or 5-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with a 6- category or 6-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with a 7-category or 7-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with an 8-category or 8-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with a 9-category or 9-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with a 10-category or 10-score system. In one embodiment, the referenced system includes percentages of cells in conjunction with any categorization or any scoring system. In one embodiment, the referenced system includes percentages of cells in conjunction with a 4-score system comprising 0 (negative for IL-23R), 1 (low/weak IL-23R expression), 2 (medium/moderate IL-23R expression), and 3 (high/strong IL-23R expression). [00390] In some aspects, the referenced system can be a ratio of the IL-23R expression to the expression of at least one reference protein. In some embodiments, the ratio could be a ratio of quantitative measurements of IL-23R expression and those of a reference protein, wherein the quantitative measurements include those described herein such as molar concentration, mole quantity, fluorescence intensity measurements of bound antibodies, luminescence intensity measurements of bound antibodies, radioactivity measurements of bound antibodies, and/or colorimetric or chromogenic measurements of bound antibodies. In other embodiments, the ratio could also be a ratio of scores assigned to IL-23R expression and the reference protein according to any scoring system provided herein. A reference protein could be a protein of ordinary cell function such as actin, GAPDH, GDI, or any protein expressed by a house-keeping gene. For example, if a test sample has a score of 3 for IL-23R expression and score of 1 for expression of actin, the ratio can be determined to be 3. [00391] In other aspects, the reference system can utilize the results of a mathematical function using one or more of the categorization, score, ratio, percentage, and quantitative measurement as input. In some embodiments, the mathematical function uses compounding, addition, multiplication, or combination these operators to combine the various inputs to produce results that provide more detailed information about IL-23R expression in the sample and/or finer gradation on the IL-23R expression scale. In one embodiment, the mathematical function calculates an H score based on the combination of percentage and a 4-score system. For example, an H-score was calculated by summing the products of the percentage of cells (0–100) having each IL-23R expression score (0=negative, 1=low/weak, 2=moderate/medium, and 3=high/strong). For example: a specimen with 10% of cells scoring 3, 30% of cells scoring 2, 20% of cells scoring 1, and 40% of cells scoring 0 would have an H-score of (3 × 10) + (2 × 30)+ (1 × 20) + (0 × 40) = 110. [00392] Therefore, as provided herein, the expression level of IL-23R can be determined using a categorization system, a scoring system, a ratio of IL-23R expression to the expression of at least one reference protein, percentage of cells in said categorization or scoring system, a quantitative measurement of IL-23R staining signal, or a result of a mathematical function using one or more of said categorization, score, ratio, percentage, and quantitative measurement as input. [00393] Most formalin-fixed tissues require an antigen retrieval step before immunohistochemical staining. Methylene bridges formed during fixation cross-link proteins and mask the epitopes of the antigens. Antigen retrieval methods break these methylene bridges and expose the epitopes, allowing antibodies to bind. In some embodiments, antigens are retrieved by a heat induced epitope retrieval (HIER) method. In other embodiments, antigens are retrieved by an enzymatic retrieval (e.g. proteolytic digestion) method. For HIER, formalin-fixed, paraffin-embedded (FFPE) tissue sections can be heated at 50°C, 55°C, 60°C, 65°C, 70°C, 75°C, 80°C, 85°C, 90°C, 95°C, 100°C, 105°C, 110°C, 115°C, 120°C, 125°C, or 130°C. The FFPE tissue section can be heated at any of these temperatures for 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 150, 180, 240, 300, 360, 420, 480, 540, 600, 660, 720, 780, 840, 900, 960, 1020, 1080, 1140, 1200, 1260, 1320, 1380, and 1440 minutes. The HIER procedure at any of the aforementioned temperatures and for any of the aforementioned durations can be performed in a solution having a pH of 2, 2.5, 3, 3.5, 4, 4.5, 5, 5.2, 5.4, 5.6, 5.8, 6.0, 6.2, 6.4, 6.6, 6.8, 7, 7.2, 7.4, 7.6, 7.8, 8, 8.2, 8.4, 8.6, 8.8, 9, 9.2, 9.4, 9.6, 9.8, 10, 10.2, 10.4, 10.6, 10.8, 11, 11.5, or 12. In some embodiments, the HIER can be performed at a temperature selected from a group consisting of 80°C, 85°C, 90°C, 95°C, 100°C, 105°C, 110°C, 115°C, for a duration selected from a group consisting of 5, 10, 15, 20, 25, 30, 35, 40, and at a pH selected from a group consisting of 8, 8.2, 8.4, 8.6, 8.8, 9, 9.2, 9.4, 9.6, 9.8, 10, 10.2, 10.4. [00394] Thus, the methods provided herein further include a step of retrieving the epitope of IL-23R by heat-induced epitope retrieval (HIER). [00395] Unlabeled antibodies, labeled antibodies and derivatives and analogs thereof, which immunospecifically bind to an IL-23R antigen can be used for diagnostic purposes to detect, diagnose, or monitor an IL-23R-mediated disease. Thus, provided herein are methods for the detection of an IL-23R-mediated disease comprising: (a) assaying the expression of an IL-23R antigen in cells or a tissue sample of a subject using one or more antibodies provided herein that immunospecifically bind to the IL-23R antigen; and (b) comparing the level of the IL-23R antigen with a control level, e.g., levels in normal tissue samples (e.g., from a patient not having an IL-23R- mediated disease, or from the same patient before disease onset), whereby an increase in the assayed level of IL-23R antigen compared to the control level of the IL-23R antigen is indicative of an IL- 23R-mediated disease. [00396] Also provided herein is a diagnostic assay for diagnosing an IL-23R-mediated disease comprising: (a) assaying for the level of an IL-23R antigen in cells or a tissue sample of an individual using one or more antibodies provided herein that immunospecifically bind to an IL-23R antigen; and (b) comparing the level of the IL-23R antigen with a control level, e.g., levels in normal tissue samples, whereby an increase in the assayed IL-23R antigen level compared to the control level of the IL-23R antigen is indicative of an IL-23R-mediated disease. In certain embodiments, provided herein is a method of treating an IL-23R-mediated disease in a subject, comprising: (a) assaying for the level of an IL-23R antigen in cells or a tissue sample of the subject using one or more antibodies provided herein that immunospecifically bind to an IL-23R antigen; and (b) comparing the level of the IL-23R antigen with a control level, e.g., levels in normal tissue samples, whereby an increase in the assayed IL-23R antigen level compared to the control level of the IL-23R antigen is indicative of an IL-23R- mediated disease. In some embodiments, the method further comprises (c) administering an effective amount of an antibody provided herein to the subject identified as having the IL-23R-mediated disease. A more definitive diagnosis of an IL-23R-mediated disease may allow health professionals to employ preventative measures or aggressive treatment earlier thereby preventing the development or further progression of the IL-23R-mediated disease. [00397] Antibodies provided herein can be used to assay IL-23R antigen levels in a biological sample using classical immunohistological methods as described herein or as known to those of skill in the art (e.g., see Jalkanen et al., 1985, J. Cell. Biol.101:976-985; and Jalkanen et al., 1987, J. Cell. Biol.105:3087-3096). Other antibody-based methods useful for detecting protein gene expression include immunoassays, such as the enzyme linked immunosorbent assay (ELISA) and the radioimmunoassay (RIA). Suitable antibody assay labels are known in the art and include enzyme labels, such as, glucose oxidase; radioisotopes, such as iodine (125I, 121I), carbon (14C), sulfur (35S), tritium (3H), indium (121In), and technetium (99Tc); luminescent labels, such as luminol; and fluorescent labels, such as fluorescein and rhodamine, and biotin. [00398] One aspect provided herein is the detection and diagnosis of an IL-23R-mediated disease in a human. In one embodiment, diagnosis comprises: a) administering (for example, parenterally, subcutaneously, or intraperitoneally) to a subject an effective amount of a labeled antibody that immunospecifically binds to an IL-23R antigen; b) waiting for a time interval following the administering for permitting the labeled antibody to concentrate at sites in the subject where the IL-23R antigen is expressed (and for unbound labeled molecule to be cleared to background level); c) determining background level; and d) detecting the labeled antibody in the subject, such that detection of labeled antibody above the background level indicates that the subject has an IL-23R-mediated disease. Background level can be determined by various methods including, comparing the amount of labeled molecule detected to a standard value previously determined for a particular system. [00399] It will be understood in the art that the size of the subject and the imaging system used will determine the quantity of imaging moiety needed to produce diagnostic images. In the case of a radioisotope moiety, for a human subject, the quantity of radioactivity injected will normally range from about 5 to 20 millicuries of 99Tc. The labeled antibody will then accumulate at the location of cells which contain the specific protein. In vivo tumor imaging is described in S.W. Burchiel et al., “Immunopharmacokinetics of Radiolabeled Antibodies and Their Fragments.” (Chapter 13 in Tumor Imaging: The Radiochemical Detection of Cancer, S.W. Burchiel and B.A. Rhodes, eds., Masson Publishing Inc. (1982). [00400] Depending on several variables, including the type of label used and the mode of administration, the time interval following the administration for permitting the labeled antibody to concentrate at sites in the subject and for unbound labeled antibody to be cleared to background level is 6 to 48 hours or 6 to 24 hours or 6 to 12 hours. In another embodiment, the time interval following administration is 5 to 20 days or 5 to 10 days. [00401] In one embodiment, monitoring of an IL-23R-mediated disease is carried out by repeating the method for diagnosing the IL-23R-mediated disease, for example, one month after initial diagnosis, six months after initial diagnosis, one year after initial diagnosis, etc. [00402] Presence of the labeled molecule can be detected in the subject using methods known in the art for in vivo scanning. These methods depend upon the type of label used. Skilled artisans will be able to determine the appropriate method for detecting a particular label. Methods and devices that may be used in the diagnostic methods provided herein include, but are not limited to, computed tomography (CT), whole body scan such as position emission tomography (PET), magnetic resonance imaging (MRI), and sonography. [00403] In a specific embodiment, the molecule is labeled with a radioisotope and is detected in the patient using a radiation responsive surgical instrument (Thurston et al., U.S. Patent No. 5,441,050). In another embodiment, the molecule is labeled with a fluorescent compound and is detected in the patient using a fluorescence responsive scanning instrument. In another embodiment, the molecule is labeled with a positron emitting metal and is detected in the patient using positron emission-tomography. In yet another embodiment, the molecule is labeled with a paramagnetic label and is detected in a patient using magnetic resonance imaging (MRI). Methods of Therapeutic Use [00404] In another aspect, provided herein is a method of treating a disease or disorder in a subject comprising administering to the subject an effective amount of an antibody or antigen binding fragment thereof provided herein. In one embodiment, the disease or disorder is an IL-23R-mediated disease or disorder. In one embodiment, the disease or disorder is an IL-23-associated disease or disorder. Also provided herein is a method of treatment of a disease or disorder, wherein the subject is administered one or more therapeutic agents in combination with the antibody or antigen-binding fragment thereof provided herein. [00405] The disclosure also relates to methods of using the antibodies provided herein to inhibit, i.e. antagonize, function of IL-23R in order to inhibit STAT activation. In some embodiments, the antibodies provided herein inhibit function of IL-23R in order to inhibit STAT3 activation. In some embodiments, the antibodies provided herein inhibit STAT3 phosphorylation. [00406] The disclosure also to a method of treating or preventing an IL-23R associated disease or disorder in a subject in need thereof, comprising administering to the subject an isolated monoclonal antibody or antigen binding fragment thereof that specifically binds IL-23R or a pharmaceutical composition of the invention. The disclosure also relates to a method of treating or preventing an autoimmune disease in a subject in need thereof, comprising administering to the subject an isolated monoclonal antibody or antigen binding fragment thereof that specifically binds IL-23R or a pharmaceutical composition of the invention. In some embodiments, the autoimmune disease is selected from subset of inflammatory diseases, which include, but are not limited to psoriasis (PSO), psoriatic arthritis (PSA), inflammatory bowel disease (IBD), Crohn's disease (CD), or ulcerative colitis (UC). [00407] The pharmaceutical composition comprises a therapeutically effective amount of an anti-IL-23R antibody or antigen binding fragment thereof. As used herein, the term “therapeutically effective amount” refers to an amount of an active ingredient or component that elicits the desired biological or medicinal response in a subject. A therapeutically effective amount can be determined empirically and in a routine manner, in relation to the stated purpose. [00408] As used herein with reference to anti-IL-23R antibodies or antigen-binding fragments thereof, a therapeutically effective amount means an amount of the anti-IL-23R antibody or antigen- binding fragment thereof that modulates an immune response in a subject in need thereof. [00409] A therapeutically effective amount refers to the amount of therapy which is sufficient to achieve one, two, three, four, or more of the following effects: (i) reduce or ameliorate the severity of the disease, disorder or condition to be treated or a symptom associated therewith; (ii) reduce the duration of the disease, disorder or condition to be treated, or a symptom associated therewith; (iii) prevent the progression of the disease, disorder or condition to be treated, or a symptom associated therewith; (iv) cause regression of the disease, disorder or condition to be treated, or a symptom associated therewith; (v) prevent the development or onset of the disease, disorder or condition to be treated, or a symptom associated therewith; (vi) prevent the recurrence of the disease, disorder or condition to be treated, or a symptom associated therewith; (vii) reduce hospitalization of a subject having the disease, disorder or condition to be treated, or a symptom associated therewith; (viii) reduce hospitalization length of a subject having the disease, disorder or condition to be treated, or a symptom associated therewith; (ix) increase the survival of a subject with the disease, disorder or condition to be treated, or a symptom associated therewith; (xi) inhibit or reduce the disease, disorder or condition to be treated, or a symptom associated therewith in a subject; and/or (xii) enhance or improve the prophylactic or therapeutic effect(s) of another therapy. [00410] The therapeutically effective amount or dosage can vary according to various factors, such as the disease, disorder or condition to be treated, the means of administration, the target site, the physiological state of the subject (including, e.g., age, body weight, health), whether the subject is a human or an animal, other medications administered, and whether the treatment is prophylactic or therapeutic. Treatment dosages are optimally titrated to optimize safety and efficacy. [00411] According to particular embodiments, the compositions described herein are formulated to be suitable for the intended route of administration to a subject. For example, the compositions described herein can be formulated to be suitable for intravenous, subcutaneous, or intramuscular administration. [00412] As used herein, the terms “treat,” “treating,” and “treatment” are all intended to refer to an amelioration or reversal of at least one measurable physical parameter related to an autoimmune disease or disorder (e.g., psoriasis), which is not necessarily discernible in the subject, but can be discernible in the subject. The terms “treat,” “treating,” and “treatment,” can also refer to causing regression, preventing the progression, or at least slowing down the progression of the disease, disorder, or condition. In a particular embodiment, “treat,” “treating,” and “treatment” refer to an alleviation, prevention of the development or onset, or reduction in the duration of one or more symptoms associated with the disease, disorder, or condition, such as an autoimmune disorder (e.g., psoriasis). In a particular embodiment, “treat,” “treating,” and “treatment” refer to prevention of the recurrence of the disease, disorder, or condition. In a particular embodiment, “treat,” “treating,” and “treatment” refer to an increase in the survival of a subject having the disease, disorder, or condition. In a particular embodiment, “treat,” “treating,” and “treatment” refer to elimination of the disease, disorder, or condition in the subject. [00413] According to particular embodiments, provided are compositions used in the treatment or prevention of an autoimmune disease. For an autoimmune therapy, the compositions can be used in combination with another treatment including, but not limited to, a chemotherapy, an anti- HLA-Cw6 mAb, anti-IL-23 mAb, an anti-TNF-alpha mAb, an anti-IL-17A mAb, other autoimmune disease drugs, an antibody-drug conjugate (ADC), or a targeted therapy. Anti-IL-23R antibodies can be used to construct bispecific antibodies with partner mAbs against HLA-Cw6, TNF-alpha, IL-17A, and/or other cell surface antigens to treat autoimmune diseases that express both IL-23R and the specific cell surface antigen. [00414] As used herein, the term “in combination,” in the context of the administration of two or more distinct therapies to a subject, refers to the use of more than one therapy. The use of the term “in combination” does not restrict the order in which therapies are administered to a subject. For example, a first therapy (e.g., a composition described herein) can be administered prior to (e.g., 5 minutes, 15 minutes, 30 minutes, 45 minutes, 1 hour, 2 hours, 4 hours, 6 hours, 12 hours, 16 hours, 24 hours, 48 hours, 72 hours, 96 hours, 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 8 weeks, or 12 weeks before), concomitantly with, or subsequent to (e.g., 5 minutes, 15 minutes, 30 minutes, 45 minutes, 1 hour, 2 hours, 4 hours, 6 hours, 12 hours, 16 hours, 24 hours, 48 hours, 72 hours, 96 hours, 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 8 weeks, or 12 weeks after) the administration of a second therapy to a subject. [00415] As used herein, in aspects the term “in combination,” in the context of the administration of two or more distinct antibodies particularly including two or more distinct IL-23R antibodies or a first IL-23R antibody and a second antibody which may bind IL-23R or which may not bind IL-23R, to a subject, refers to the use of more than one antibody together. The use of the term “in combination” does not restrict the order in which the antibodies are provided in a particular context or administered to a subject. For example, a first antibody (e.g., a composition comprising an IL-23R antibody described herein) can be administered prior to (e.g., 5 minutes, 15 minutes, 30 minutes, 45 minutes, 1 hour, 2 hours, 4 hours, 6 hours, 12 hours, 16 hours, 24 hours, 48 hours, 72 hours, 96 hours, 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 8 weeks, or 12 weeks before), concomitantly with, or subsequent to (e.g., 5 minutes, 15 minutes, 30 minutes, 45 minutes, 1 hour, 2 hours, 4 hours, 6 hours, 12 hours, 16 hours, 24 hours, 48 hours, 72 hours, 96 hours, 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 8 weeks, or 12 weeks after) the administration of a second antibody to a subject. [00416] Methods of administration and dosing is described in more detail in below. [00417] In another aspect, provided herein is the use of the antibody or antigen binding fragment thereof provided herein in the manufacture of a medicament for treating a disease or disorder in a subject. [00418] In another aspect, provided herein is the use of a pharmaceutical composition provided herein in the manufacture of a medicament for treating a disease or disorder in a subject. [00419] In another aspect, provided herein is the use of an antibody or antigen binding fragment thereof provided herein in the manufacture of a medicament, wherein the medicament is for use in a method for detecting the presence of an IL-23R in a biological sample, the method comprising contacting the biological sample with the antibody under conditions permissive for binding of the antibody to the IL-23R protein, and detecting whether a complex is formed between the antibody and the IL-23R protein. [00420] In a specific embodiment, provided herein is a composition for use in the prevention and/or treatment of a disease or condition comprising an antibody or antigen binding fragment thereof provided herein. In one embodiment, provided herein is a composition for use in the prevention of a disease or condition, wherein the composition comprises an antibody or antigen binding fragment thereof provided herein. In one embodiment, provided herein is a composition for use in the treatment of a disease or condition, wherein the composition comprises an antibody or antigen binding fragment thereof provided herein. In some embodiments, the disease or condition is an IL-23R- mediated disease. In some embodiments, the disease or condition is an IL-23-mediated disease. In some embodiments, the disease or disorder is associated with IL-23R. In some embodiments, the disease or disorder is an autoimmune disease. In certain embodiments, the disease or disorder is multiple sclerosis, asthma, rheumatoid arthritis, inflammatory bowel disease (IBD), juvenile IBD, adolescent IBD, Crohn's disease, sarcoidosis, systemic elitematodes, ankylosing spondylitis, Autoimmune inflammation such as inflammation (axial spondylitic arthritis), psoriatic arthritis, or psoriasis and related diseases and disorders. In certain embodiments, the disease or disorder is psoriasis (eg, psoriasis vulgaris, guttate psoriasis), inverse psoriasis, pustular psoriasis, palmo-plantar, Psoriasis, psoriasis vulgaris, or psoriatic psoriasis, atopic dermatitis, acne ectopica, ulcerative colitis, Crohn's disease, Celiac's disease Sexual sprue, enteropathy with seronegative arthritis, microscopic colitis, collagen-accumulating colitis, eosinophilia gastroenteritis / esophagitis, colitis associated with radiation or chemotherapy, leukocyte adhesion deficiency-1 Psoriasis with congenital immunity disorders, chronic granulomatosis, glycogenosis type 1b, Hermannsky-Padrac syndrome, Chediac- East syndrome, Wiscot-Aldrich syndrome, rectal colon resection and ileal anastomosis, Later ileal psoriasis, gastrointestinal cancer, pancreatitis, insulin-dependent diabetes, mammary psoriasis, psoriasis, bile ductitis, primary biliary cirrhosis, virus-related enteropathy, periductitis, chronic bronchitis, chronic sinusitis, asthma, Psoriasis, or implant-to-host disease. In some embodiments, the disease or disorder is selected from subset of inflammatory diseases, which include, but are not limited to psoriasis (PSO), psoriatic arthritis (PSA), inflammatory bowel disease (IBD), Crohn's disease (CD), or ulcerative colitis (UC). [00421] In certain embodiments, the subject is a subject in need thereof. In some embodiments, the subject has the disease or condition. In other embodiments, the subject is at risk of having the disease or condition. In some embodiments, the administration results in the prevention, management, treatment or amelioration of the disease or condition. [00422] In one embodiment, provided herein is a composition for use in the prevention and/or treatment of a symptom of a disease or condition, wherein the composition comprises an antibody or antigen binding fragment thereof provided herein. In one embodiment, provided herein is a composition for use in the prevention of a symptom of a disease or condition, wherein the composition comprises an antibody or antigen binding fragment thereof provided herein. In one embodiment, provided herein is a composition for use in the treatment of a symptom of a disease or condition, wherein the composition comprises an antibody or antigen binding fragment thereof provided herein. In some embodiments, the disease or condition is an IL-23R-mediated and/or IL-23 mediated disease. In some embodiments, the disease or disorder is associated with IL-23R. In some embodiments, the disease or disorder is an autoimmune disease. In certain embodiments, the disease or disorder is multiple sclerosis, asthma, rheumatoid arthritis, inflammatory bowel disease (IBD), juvenile IBD, adolescent IBD, Crohn's disease, sarcoidosis, systemic elitematodes, ankylosing spondylitis, Autoimmune inflammation such as inflammation (axial spondylotic arthritis), psoriatic arthritis, or psoriasis and related diseases and disorders. In certain embodiments, the disease or disorder is psoriasis (eg, psoriasis vulgaris, guttate psoriasis), inverse psoriasis, pustular psoriasis, palmo-plantar, Psoriasis, psoriasis vulgaris, or psoriatic psoriasis, atopic dermatitis, acne ectopica, ulcerative colitis, Crohn's disease, Celiac's disease Sexual sprue, enteropathy with seronegative arthritis, microscopic colitis, collagen-accumulating colitis, eosinophilia gastroenteritis / esophagitis, colitis associated with radiation or chemotherapy, leukocyte adhesion deficiency-1 Psoriasis with congenital immunity disorders, chronic granulomatosis, glycogenosis type 1b, Hermannsky-Padrac syndrome, Chediac-East syndrome, Wiscot-Aldrich syndrome, rectal colon resection and ileal anastomosis, Later ileal psoriasis, gastrointestinal cancer, pancreatitis, insulin-dependent diabetes, mammary psoriasis, psoriasis, bile ductitis, primary biliary cirrhosis, virus-related enteropathy, periductitis, chronic bronchitis, chronic sinusitis, asthma, Psoriasis, or implant-to-host disease. In some embodiments, the disease or disorder is selected from subset of inflammatory diseases, which include, but are not limited to psoriasis (PSO), psoriatic arthritis (PSA), inflammatory bowel disease (IBD), Crohn's disease (CD), or ulcerative colitis (UC). In certain embodiments, the subject is a subject in need thereof. In some embodiments, the subject has the disease or condition. In other embodiments, the subject is at risk of having the disease or condition. In some embodiments, the administration results in the prevention or treatment of the symptom of the disease or condition. [00423] In another embodiment, provided herein is a method of preventing and/or treating a disease or condition in a subject, comprising administering an effective amount of an antibody or antigen binding fragment thereof provided herein. In one embodiment, provided herein is a method of preventing a disease or condition in a subject, comprising administering an effective amount of an antibody or antigen binding fragment thereof provided herein. In one embodiment, provided herein is a method of treating a disease or condition in a subject, comprising administering an effective amount of an antibody or antigen binding fragment thereof provided herein. In some embodiments, the disease or condition is an IL-23R-mediated and/or IL-23 mediated disease. In some embodiments, the disease or disorder is associated with IL-23R. In some embodiments, the disease or disorder is an autoimmune disease. In certain embodiments, the disease or disorder is multiple sclerosis, asthma, rheumatoid arthritis, inflammatory bowel disease (IBD), juvenile IBD, adolescent IBD, Crohn's disease, sarcoidosis, systemic elitematodes, ankylosing spondylitis, Autoimmune inflammation such as inflammation (axial spondylotic arthritis), psoriatic arthritis, or psoriasis and related diseases and disorders. In certain embodiments, the disease or disorder is psoriasis (eg, psoriasis vulgaris, guttate psoriasis), inverse psoriasis, pustular psoriasis, palmo-plantar, Psoriasis, psoriasis vulgaris, or psoriatic psoriasis, atopic dermatitis, acne ectopica, ulcerative colitis, Crohn's disease, Celiac's disease Sexual sprue, enteropathy with seronegative arthritis, microscopic colitis, collagen-accumulating colitis, eosinophilia gastroenteritis / esophagitis, colitis associated with radiation or chemotherapy, leukocyte adhesion deficiency-1 Psoriasis with congenital immunity disorders, chronic granulomatosis, glycogenosis type 1b, Hermannsky-Padrac syndrome, Chediac-East syndrome, Wiscot-Aldrich syndrome, rectal colon resection and ileal anastomosis, Later ileal psoriasis, gastrointestinal cancer, pancreatitis, insulin-dependent diabetes, mammary psoriasis, psoriasis, bile ductitis, primary biliary cirrhosis, virus-related enteropathy, periductitis, chronic bronchitis, chronic sinusitis, asthma, Psoriasis, or implant-to-host disease. In some embodiments, the disease or disorder is selected from subset of inflammatory diseases, which include, but are not limited to psoriasis (PSO), psoriatic arthritis (PSA), inflammatory bowel disease (IBD), Crohn's disease (CD), or ulcerative colitis (UC). In certain embodiments, the subject is a subject in need thereof. In some embodiments, the subject has the disease or condition. In other embodiments, the subject is at risk of having the disease or condition. In some embodiments, the administration results in the prevention or treatment of the disease or condition. [00424] In another embodiment, provided herein is a method of preventing and/or treating a symptom of a disease or condition in a subject, comprising administering an effective amount of an antibody or antigen binding fragment thereof provided herein. In one embodiment, provided herein is a method of preventing a symptom of a disease or condition in a subject, comprising administering an effective amount of an antibody or antigen binding fragment thereof provided herein. In one embodiment, provided herein is a method of treating a symptom of a disease or condition in a subject, comprising administering an effective amount of an antibody or antigen binding fragment thereof provided herein. In some embodiments, the disease or condition is an IL-23R-mediated and/or IL-23 mediated disease. In some embodiments, the disease or disorder is associated with IL-23R. In some embodiments, the disease or disorder is an autoimmune disease. In certain embodiments, the disease or disorder is multiple sclerosis, asthma, rheumatoid arthritis, inflammatory bowel disease (IBD), juvenile IBD, adolescent IBD, Crohn's disease, sarcoidosis, systemic elitematodes, ankylosing spondylitis, Autoimmune inflammation such as inflammation (axial spondylotic arthritis), psoriatic arthritis, or psoriasis and related diseases and disorders. In certain embodiments, the disease or disorder is psoriasis (eg, psoriasis vulgaris, guttate psoriasis), inverse psoriasis, pustular psoriasis, palmo-plantar, Psoriasis, psoriasis vulgaris, or psoriatic psoriasis, atopic dermatitis, acne ectopica, ulcerative colitis, Crohn's disease, Celiac's disease Sexual sprue, enteropathy with seronegative arthritis, microscopic colitis, collagen-accumulating colitis, eosinophilia gastroenteritis / esophagitis, colitis associated with radiation or chemotherapy, leukocyte adhesion deficiency-1 Psoriasis with congenital immunity disorders, chronic granulomatosis, glycogenosis type 1b, Hermannsky-Padrac syndrome, Chediac-East syndrome, Wiscot-Aldrich syndrome, rectal colon resection and ileal anastomosis, Later ileal psoriasis, gastrointestinal cancer, pancreatitis, insulin-dependent diabetes, mammary psoriasis, psoriasis, bile ductitis, primary biliary cirrhosis, virus-related enteropathy, periductitis, chronic bronchitis, chronic sinusitis, asthma, Psoriasis, or implant-to-host disease. In some embodiments, the disease or disorder is selected from subset of inflammatory diseases, which include, but are not limited to psoriasis (PSO), psoriatic arthritis (PSA), inflammatory bowel disease (IBD), Crohn's disease (CD), or ulcerative colitis (UC). In certain embodiments, the subject is a subject in need thereof. In some embodiments, the subject has the disease or condition. In other embodiments, the subject is at risk of having the disease or condition. In some embodiments, the administration results in the prevention or treatment of the symptom of the disease or condition. [00425] Also provided herein are methods of preventing and/or treating a disease or condition by administrating to a subject of an effective amount of an antibody or antigen binding fragment thereof provided herein, or pharmaceutical composition comprising an antibody or antigen binding fragment thereof provided herein. In one aspect, the antibody or antigen binding fragment thereof is substantially purified (i.e., substantially free from substances that limit its effect or produce undesired side-effects). The subject administered a therapy can be a mammal such as non-primate (e.g., cows, pigs, horses, cats, dogs, rats etc.) or a primate (e.g., a monkey, such as a cynomolgus macaque monkey, or a human). In a one embodiment, the subject is a human. In another embodiment, the subject is a human with a disease or condition. [00426] Various delivery systems are known and can be used to administer a prophylactic or therapeutic agent (e.g., an antibody or antigen binding fragment thereof provided herein), including, but not limited to, encapsulation in liposomes, microparticles, microcapsules, recombinant cells capable of expressing the antibody or antigen binding fragment thereof, receptor-mediated endocytosis (see, e.g., Wu and Wu, J. Biol. Chem.262:4429-4432 (1987)), construction of a nucleic acid as part of a retroviral or other vector, etc. Methods of administering a prophylactic or therapeutic agent (e.g., an antibody or antigen binding fragment thereof provided herein), or pharmaceutical composition include, but are not limited to, parenteral administration (e.g., intradermal, intramuscular, intraperitoneal, intravenous and subcutaneous), epidural, and mucosal (e.g., intranasal and oral routes). In a specific embodiment, a prophylactic or therapeutic agent (e.g., an antibody or antigen binding fragment thereof provided herein), or a pharmaceutical composition is administered intranasally, intramuscularly, intravenously, or subcutaneously. The prophylactic or therapeutic agents, or compositions may be administered by any convenient route, for example by infusion or bolus injection, by absorption through epithelial or mucocutaneous linings (e.g., oral mucosa, intranasal mucosa, rectal and intestinal mucosa, etc.) and may be administered together with other biologically active agents. Administration can be systemic or local. In addition, pulmonary administration can also be employed, e.g., by use of an inhaler or nebulizer, and formulation with an aerosolizing agent. See, e.g., U.S. Patent Nos.6,019,968, 5,985,320, 5,985,309, 5,934,272, 5,874,064, 5,855,913, 5,290,540, and 4,880,078; and PCT Publication Nos. WO 92/19244, WO 97/32572, WO 97/44013, WO 98/31346, and WO 99/66903, each of which is incorporated herein by reference their entirety. [00427] In some embodiment, nanoparticles that contain anti-IL-23R antibodies are used to deliver therapeutic agents to IL-23R expressing cells. In some embodiment, the therapeutic agents antagonize a different target other than IL-23R (e.g. siRNA against TNFa, etc) . [00428] In a specific embodiment, it may be desirable to administer a prophylactic or therapeutic agent, or a pharmaceutical composition provided herein locally to the area in need of treatment. This may be achieved by, for example, and not by way of limitation, local infusion, by topical administration (e.g., by intranasal spray), by injection, or by means of an implant, said implant being of a porous, non-porous, or gelatinous material, including membranes, such as sialastic membranes, or fibers. In some embodiments, when administering an antibody or antigen binding fragment thereof provided herein, care must be taken to use materials to which the antibody or antigen binding fragment thereof does not absorb. [00429] In another embodiment, a prophylactic or therapeutic agent, or a composition provided herein can be delivered in a vesicle, in particular a liposome (see Langer, 1990, Science 249:1527-1533; Treat et al., in Liposomes in the Therapy of Infectious Disease and Cancer, Lopez- Berestein and Fidler (eds.), Liss, New York, pp.353- 365 (1989); Lopez-Berestein, ibid., pp.317-327; see generally ibid.). [00430] In another embodiment, a prophylactic or therapeutic agent, or a composition provided herein can be delivered in a controlled release or sustained release system. In one embodiment, a pump may be used to achieve controlled or sustained release (see Langer, supra; Sefton, 1987, CRC Crit. Ref. Biomed. Eng.14:20; Buchwald et al., 1980, Surgery 88:507; Saudek et al., 1989, N. Engl. J. Med.321:574). In another embodiment, polymeric materials can be used to achieve controlled or sustained release of a prophylactic or therapeutic agent (e.g., an antibody provided herein) or a composition provided herein (see e.g., Medical Applications of Controlled Release, Langer and Wise (eds.), CRC Pres., Boca Raton, Florida (1974); Controlled Drug Bioavailability, Drug Product Design and Performance, Smolen and Ball (eds.), Wiley, New York (1984); Ranger and Peppas, 1983, J., Macromol. Sci. Rev. Macromol. Chem.23:61; see also Levy et al., 1985, Science 228:190; During et al., 1989, Ann. Neurol.25:351; Howard et al., 1989, J. Neurosurg.71:105); U.S. Patent No.5,679,377; U.S. Patent No.5,916,597; U.S. Patent No. 5,912,015; U.S. Patent No.5,989,463; U.S. Patent No.5,128,326; PCT Publication No. WO 99/15154; and PCT Publication No. WO 99/20253. Examples of polymers used in sustained release formulations include, but are not limited to, poly(2-hydroxy ethyl methacrylate), poly(methyl methacrylate), poly(acrylic acid), poly(ethylene-co-vinyl acetate), poly(methacrylic acid), polyglycolides (PLG), polyanhydrides, poly(N-vinyl pyrrolidone), poly(vinyl alcohol), polyacrylamide, poly(ethylene glycol), polylactides (PLA), poly(lactide-co-glycolides) (PLGA), and polyorthoesters. In an embodiment, the polymer used in a sustained release formulation is inert, free of leachable impurities, stable on storage, sterile, and biodegradable. In yet another embodiment, a controlled or sustained release system can be placed in proximity of the therapeutic target, i.e., the nasal passages or lungs, thus requiring only a fraction of the systemic dose (see, e.g., Goodson, in Medical Applications of Controlled Release, supra, vol.2, pp.115-138 (1984)). Controlled release systems are discussed in the review by Langer (1990, Science 249:1527-1533). Any technique known to one of skill in the art can be used to produce sustained release formulations comprising one or more antibody or antigen binding fragment thereof provided herein. See, e.g., U.S. Patent No.4,526,938, PCT publication WO 91/05548, PCT publication WO 96/20698, Ning et al., 1996, “Intratumoral Radioimmunotherapy of a Human Colon Cancer Xenograft Using a Sustained-Release Gel,” Radiotherapy & Oncology 39:179- 189, Song et al., 1995, “Antibody Mediated Lung Targeting of Long-Circulating Emulsions,” PDA Journal of Pharmaceutical Science & Technology 50:372-397, Cleek et al., 1997, “Biodegradable Polymeric Carriers for a bFGF Antibody for Cardiovascular Application,” Pro. Int’l. Symp. Control. Rel. Bioact. Mater.24:853-854, and Lam et al., 1997, “Microencapsulation of Recombinant Humanized Monoclonal Antibody for Local Delivery,” Proc. Int’l. Symp. Control Rel. Bioact. Mater.24:759-760, each of which is incorporated herein by reference in their entirety. [00431] In a specific embodiment, where the composition provided herein is a nucleic acid encoding a prophylactic or therapeutic agent (e.g., an antibody or antigen binding fragment thereof provided herein), the nucleic acid can be administered in vivo to promote expression of its encoded prophylactic or therapeutic agent, by constructing it as part of an appropriate nucleic acid expression vector and administering it so that it becomes intracellular, e.g., by use of a retroviral vector (see U.S. Patent No.4,980,286), or by direct injection, or by use of microparticle bombardment (e.g., a gene gun; Biolistic, Dupont), or coating with lipids or cell surface receptors or transfecting agents, or by administering it in linkage to a homeobox-like peptide which is known to enter the nucleus (see, e.g., Joliot et al., 1991, Proc. Natl. Acad. Sci. USA 88:1864-1868), etc. Alternatively, a nucleic acid can be introduced intracellularly and incorporated within host cell DNA for expression by homologous recombination. [00432] In a specific embodiment, a composition provided herein comprises one, two or more antibodies or antigen binding fragments thereof provided herein. In another embodiment, a composition provided herein comprises one, two or more antibodies or antigen binding fragments thereof provided herein and a prophylactic or therapeutic agent other than an antibody or antigen binding fragment thereof provided herein. In one embodiment, the agents are known to be useful for or have been or are currently used for the prevention, management, treatment and/or amelioration of a disease or condition. In addition to prophylactic or therapeutic agents, the compositions provided herein may also comprise an excipient. [00433] The compositions provided herein include bulk drug compositions useful in the manufacture of pharmaceutical compositions (e.g., compositions that are suitable for administration to a subject or patient) that can be used in the preparation of unit dosage forms. In an embodiment, a composition provided herein is a pharmaceutical composition. Such compositions comprise a prophylactically or therapeutically effective amount of one or more prophylactic or therapeutic agents (e.g., an antibody or antigen binding fragment thereof provided herein or other prophylactic or therapeutic agent), and a pharmaceutically acceptable excipient. The pharmaceutical compositions can be formulated to be suitable for the route of administration to a subject. [00434] In a specific embodiment, the term “excipient” can also refer to a diluent, adjuvant (e.g., Freunds’ adjuvant (complete or incomplete) or vehicle. Pharmaceutical excipients can be sterile liquids, such as water and oils, including those of petroleum, animal, vegetable or synthetic origin, such as peanut oil, soybean oil, mineral oil, sesame oil and the like. Water is an exemplary excipient when the pharmaceutical composition is administered intravenously. Saline solutions and aqueous dextrose and glycerol solutions can also be employed as liquid excipients, particularly for injectable solutions. Suitable pharmaceutical excipients include starch, glucose, lactose, sucrose, gelatin, malt, rice, flour, chalk, silica gel, sodium stearate, glycerol monostearate, talc, sodium chloride, dried skim milk, glycerol, propylene, glycol, water, ethanol and the like. The composition, if desired, can also contain minor amounts of wetting or emulsifying agents, or pH buffering agents. These compositions can take the form of solutions, suspensions, emulsion, tablets, pills, capsules, powders, sustained- release formulations and the like. Oral formulation can include standard excipients such as pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharine, cellulose, magnesium carbonate, etc. Examples of suitable pharmaceutical excipients are described in Remington’s Pharmaceutical Sciences (1990) Mack Publishing Co., Easton, PA. Such compositions will contain a prophylactically or therapeutically effective amount of the antibody or antigen binding fragment thereof provided herein, such as in purified form, together with a suitable amount of excipient so as to provide the form for proper administration to the patient. The formulation should suit the mode of administration. [00435] In an embodiment, the composition is formulated in accordance with routine procedures as a pharmaceutical composition adapted for intravenous administration to human beings. Typically, compositions for intravenous administration are solutions in sterile isotonic aqueous buffer. Where necessary, the composition may also include a solubilizing agent and a local anesthetic such as lignocamne to ease pain at the site of the injection. Such compositions, however, may be administered by a route other than intravenous. [00436] Generally, the ingredients of compositions provided herein are supplied either separately or mixed together in unit dosage form, for example, as a dry lyophilized powder or water free concentrate in a hermetically sealed container such as an ampoule or sachette indicating the quantity of active agent. Where the composition is to be administered by infusion, it can be dispensed with an infusion bottle containing sterile pharmaceutical grade water or saline. Where the composition is administered by injection, an ampoule of sterile water for injection or saline can be provided so that the ingredients may be mixed prior to administration. [00437] An antibody or antigen binding fragment thereof provided herein can be packaged in a hermetically sealed container such as an ampoule or sachette indicating the quantity of antibody. In one embodiment, the antibody or antigen binding fragment thereof is supplied as a dry sterilized lyophilized powder or water free concentrate in a hermetically sealed container and can be reconstituted, e.g., with water or saline to the appropriate concentration for administration to a subject. The lyophilized antibody or antigen binding fragment thereof can be stored at between 2 and 8°C in its original container and the antibody or antigen binding fragment thereof can be administered within 12 hours, such as within 6 hours, within 5 hours, within 3 hours, or within 1 hour after being reconstituted. In an alternative embodiment, an antibody or antigen binding fragment thereof provided herein is supplied in liquid form in a hermetically sealed container indicating the quantity and concentration of the antibody. [00438] The compositions provided herein can be formulated as neutral or salt forms. Pharmaceutically acceptable salts include those formed with anions such as those derived from hydrochloric, phosphoric, acetic, oxalic, tartaric acids, etc., and those formed with cations such as those derived from sodium, potassium, ammonium, calcium, ferric hydroxides, isopropylamine, triethylamine, 2-ethylamino ethanol, histidine, procaine, etc. [00439] The amount of a prophylactic or therapeutic agent (e.g., an antibody or antigen binding fragment thereof provided herein), or a composition provided herein that will be effective in the prevention and/or treatment of a disease or condition can be determined by standard clinical techniques. In addition, in vitro assays may optionally be employed to help identify optimal dosage ranges. The precise dose to be employed in the formulation will also depend on the route of administration, and the seriousness of a disease or condition, and should be decided according to the judgment of the practitioner and each patient’s circumstances. [00440] Effective doses may be extrapolated from dose-response curves derived from in vitro or animal model test systems. [00441] In certain embodiments, the route of administration for a dose of an antibody or antigen binding fragment thereof provided herein to a patient is intranasal, intramuscular, intravenous, subcutaneous, or a combination thereof, but other routes described herein are also acceptable. Each dose may or may not be administered by an identical route of administration. In some embodiments, an antibody or antigen binding fragment thereof provided herein may be administered via multiple routes of administration simultaneously or subsequently to other doses of the same or a different antibody or antigen binding fragment thereof provided herein. [00442] In certain embodiments, the antibody or antigen binding fragment thereof provided herein are administered prophylactically or therapeutically to a subject. The antibody or antigen binding fragment thereof provided herein can be prophylactically or therapeutically administered to a subject so as to prevent, lessen or ameliorate a disease or symptom thereof. Pharmaceutical Compositions [00443] In one aspect, the present disclosure further provides pharmaceutical compositions comprising at least one antibody or antigen binding fragment thereof of the present disclosure. In some embodiments, a pharmaceutical composition comprises therapeutically effective amount of an antibody or antigen binding fragment thereof provided herein and a pharmaceutically acceptable excipient. [00444] Pharmaceutical compositions comprising an antibody or antigen binding fragment thereof are prepared for storage by mixing the fusion protein having the desired degree of purity with optional physiologically acceptable excipients (see, e.g., Remington, Remington’s Pharmaceutical Sciences (18th ed.1980)) in the form of aqueous solutions or lyophilized or other dried forms. [00445] The antibody or antigen binding fragment thereof of the present disclosure may be formulated in any suitable form for delivery to a target cell/tissue, e.g., as microcapsules or macroemulsions (Remington, supra; Park et al., 2005, Molecules 10:146-61; Malik et al., 2007, Curr. Drug. Deliv.4:141-51), as sustained release formulations (Putney and Burke, 1998, Nature Biotechnol.16:153-57), or in liposomes (Maclean et al., 1997, Int. J. Oncol.11:325-32; Kontermann, 2006, Curr. Opin. Mol. Ther.8:39-45). [00446] An antibody or antigen binding fragment thereof provided herein can also be entrapped in microcapsule prepared, for example, by coacervation techniques or by interfacial polymerization, for example, hydroxymethylcellulose or gelatin-microcapsule and poly- (methylmethacylate) microcapsule, respectively, in colloidal drug delivery systems (for example, liposomes, albumin microspheres, microemulsions, nano-particles, and nanocapsules) or in macroemulsions. Such techniques are disclosed, for example, in Remington, supra. [00447] Various compositions and delivery systems are known and can be used with an antibody or antigen binding fragment thereof as described herein, including, but not limited to, encapsulation in liposomes, microparticles, microcapsules, recombinant cells capable of expressing the antibody or antigen binding fragment thereof, receptor-mediated endocytosis (see, e.g., Wu and Wu, 1987, J. Biol. Chem.262:4429-32), construction of a nucleic acid as part of a retroviral or other vector, etc. In another embodiment, a composition can be provided as a controlled release or sustained release system. In one embodiment, a pump may be used to achieve controlled or sustained release (see, e.g., Langer, supra; Sefton, 1987, Crit. Ref. Biomed. Eng.14:201-40; Buchwald et al., 1980, Surgery 88:507-16; and Saudek et al., 1989, N. Engl. J. Med.321:569-74). In another embodiment, polymeric materials can be used to achieve controlled or sustained release of a prophylactic or therapeutic agent (e.g., an antibody or antigen binding fragment thereof as described herein) or a composition provided herein (see, e.g., Medical Applications of Controlled Release (Langer and Wise eds., 1974); Controlled Drug Bioavailability, Drug Product Design and Performance (Smolen and Ball eds., 1984); Ranger and Peppas, 1983, J. Macromol. Sci. Rev. Macromol. Chem.23:61-126; Levy et al., 1985, Science 228:190-92; During et al., 1989, Ann. Neurol.25:351-56; Howard et al., 1989, J. Neurosurg.71:105-12; U.S. Pat. Nos.5,679,377; 5,916,597; 5,912,015; 5,989,463; and 5,128,326; PCT Publication Nos. WO 99/15154 and WO 99/20253). Examples of polymers used in sustained release formulations include, but are not limited to, poly(2-hydroxy ethyl methacrylate), poly(methyl methacrylate), poly(acrylic acid), poly(ethylene- co-vinyl acetate), poly(methacrylic acid), polyglycolides (PLG), polyanhydrides, poly(N-vinyl pyrrolidone), poly(vinyl alcohol), polyacrylamide, poly(ethylene glycol), polylactides (PLA), poly(lactide-co-glycolides) (PLGA), and polyorthoesters. In one embodiment, the polymer used in a sustained release formulation is inert, free of leachable impurities, stable on storage, sterile, and biodegradable. [00448] In yet another embodiment, a controlled or sustained release system can be placed in proximity of a particular target tissue, for example, the nasal passages or lungs, thus requiring only a fraction of the systemic dose (see, e.g., Goodson, Medical Applications of Controlled Release Vol.2, 115-38 (1984)). Controlled release systems are discussed, for example, by Langer, 1990, Science 249:1527-33. Any technique known to one of skill in the art can be used to produce sustained release formulations comprising one or more antibody or antigen binding fragment thereof as described herein (see, e.g., U.S. Pat. No.4,526,938, PCT publication Nos. WO 91/05548 and WO 96/20698, Ning et al., 1996, Radiotherapy & Oncology 39:179-89; Song et al., 1995, PDA J. of Pharma. Sci. & Tech.50:372-97; Cleek et al., 1997, Pro. Int’l. Symp. Control. Rel. Bioact. Mater.24:853-54; and Lam et al., 1997, Proc. Int’l. Symp. Control Rel. Bioact. Mater.24:759-60). Gene Therapy [00449] In a specific embodiment, nucleic acids comprising sequences encoding antibodies or functional derivatives thereof, are administered to a subject for use in a method provided herein, for example, to prevent, manage, treat and/or ameliorate an IL-23R-mediated disease, disorder or condition, by way of gene therapy. Such therapy encompasses that performed by the administration to a subject of an expressed or expressible nucleic acid. In an embodiment, the nucleic acids produce their encoded antibody, and the antibody mediates a prophylactic or therapeutic effect. [00450] Any of the methods for recombinant gene expression (or gene therapy) available in the art can be used. [00451] For general review of the methods of gene therapy, see Goldspiel et al., 1993, Clinical Pharmacy 12:488-505; Wu and Wu, 1991, Biotherapy 3:87-95; Tolstoshev, 1993, Ann. Rev. Pharmacol. Toxicol.32:573-596; Mulligan, 1993, Science 260:926-932; and Morgan and Anderson, 1993, Ann. Rev. Biochem.62:191-217; May, 1993, TIBTECH 11(5):155-215. Methods commonly known in the art of recombinant DNA technology which can be used are described in Ausubel et al. (eds.), Current Protocols in Molecular Biology, John Wiley & Sons, NY (1993); and Kriegler, Gene Transfer and Expression, A Laboratory Manual, Stockton Press, NY (1990). [00452] In a specific embodiment, a composition comprises nucleic acids encoding an antibody provided herein, the nucleic acids being part of an expression vector that expresses the antibody or chimeric proteins or heavy or light chains thereof in a suitable host. In particular, such nucleic acids have promoters, such as heterologous promoters, operably linked to the antibody coding region, the promoter being inducible or constitutive, and, optionally, tissue-specific. In another particular embodiment, nucleic acid molecules are used in which the antibody coding sequences and any other desired sequences are flanked by regions that promote homologous recombination at a desired site in the genome, thus providing for intrachromosomal expression of the antibody encoding nucleic acids (Koller and Smithies, 1989, Proc. Natl. Acad. Sci. USA 86:8932-8935; Zijlstra et al., 1989, Nature 342:435-438). [00453] Delivery of the nucleic acids into a subject can be either direct, in which case the subject is directly exposed to the nucleic acid or nucleic acid-carrying vectors, or indirect, in which case, cells are first transformed with the nucleic acids in vitro, then transplanted into the subject. These two approaches are known, respectively, as in vivo or ex vivo gene therapy. [00454] In a specific embodiment, the nucleic acid sequences are directly administered in vivo, where the sequences are expressed to produce the encoded product. This can be accomplished by any of numerous methods known in the art, e.g., by constructing them as part of an appropriate nucleic acid expression vector and administering the vector so that the sequences become intracellular, e.g., by infection using defective or attenuated retroviral or other viral vectors (see U.S. Patent No.4,980,286), or by direct injection of naked DNA, or by use of microparticle bombardment (e.g., a gene gun; Biolistic, Dupont), or coating with lipids or cell surface receptors or transfecting agents, encapsulation in liposomes, microparticles, or microcapsules, or by administering them in linkage to a peptide which is known to enter the nucleus, by administering it in linkage to a ligand subject to receptor-mediated endocytosis (see, e.g., Wu and Wu, 1987, J. Biol. Chem.262:4429-4432) (which can be used to target cell types specifically expressing the receptors), etc. In another embodiment, nucleic acid-ligand complexes can be formed in which the ligand comprises a fusogenic viral peptide to disrupt endosomes, allowing the nucleic acid to avoid lysosomal degradation. In yet another embodiment, the nucleic acid can be targeted in vivo for cell specific uptake and expression, by targeting a specific receptor (see, e.g., PCT Publications WO 92/06180; WO 92/22635; WO 92/20316; W093/14188, WO 93/20221). Alternatively, the nucleic acid can be introduced intracellularly and incorporated within host cell DNA for expression, by homologous recombination (Koller and Smithies, 1989, Proc. Natl. Acad. Sci. USA 86:8932-8935; and Zijlstra et al., 1989, Nature 342:435-438). [00455] In a specific embodiment, viral vectors that contains nucleic acid sequences encoding an antibody are used. For example, a retroviral vector can be used (see Miller et al., 1993, Meth. Enzymol.217:581-599). These retroviral vectors contain the components necessary for the correct packaging of the viral genome and integration into the host cell DNA. The nucleic acid sequences encoding the antibody to be used in gene therapy can be cloned into one or more vectors, which facilitates delivery of the gene into a subject. More detail about retroviral vectors can be found in Boesen et al., 1994, Biotherapy 6:291-302, which describes the use of a retroviral vector to deliver the MDR1 gene to hematopoietic stem cells in order to make the stem cells more resistant to chemotherapy. Other references illustrating the use of retroviral vectors in gene therapy are: Clowes et al., 1994, J. Clin. Invest.93:644-651; Klein et al., 1994, Blood 83:1467-1473; Salmons and Gunzberg, 1993, Human Gene Therapy 4:129-141; and Grossman and Wilson, 1993, Curr. Opin. in Genetics and Devel.3:110-114. [00456] Adenoviruses are other viral vectors that can be used in the recombinant production of antibodies. Adenoviruses are especially attractive vehicles for delivering genes to respiratory epithelia. Adenoviruses naturally infect respiratory epithelia where they cause a mild disease. Other targets for adenovirus-based delivery systems are liver, the central nervous system, endothelial cells, and muscle. Adenoviruses have the advantage of being capable of infecting non-dividing cells. Kozarsky and Wilson, 1993, Current Opinion in Genetics and Development 3:499-503 present a review of adenovirus-based gene therapy. Bout et al., 1994, Human Gene Therapy 5:3-10 demonstrated the use of adenovirus vectors to transfer genes to the respiratory epithelia of rhesus monkeys. Other instances of the use of adenoviruses in gene therapy can be found in Rosenfeld et al., 1991, Science 252:431-434; Rosenfeld et al., 1992, Cell 68:143-155; Mastrangeli et al., 1993, J. Clin. Invest.91:225-234; PCT Publication W094/12649; and Wang et al., 1995, Gene Therapy 2:775-783. In a specific embodiment, adenovirus vectors are used. [00457] Adeno-associated virus (AAV) can also be utilized (Walsh et al., 1993, Proc. Soc. Exp. Biol. Med.204:289-300; and U.S. Patent No.5,436,146). In a specific embodiment, AAV vectors are used to express an anti-IL-23R antibody as provided herein. In certain embodiments, the AAV comprises a nucleic acid encoding a VH domain. In other embodiments, the AAV comprises a nucleic acid encoding a VL domain. In certain embodiments, the AAV comprises a nucleic acid encoding a VH domain and a VL domain. In some embodiments of the methods provided herein, a subject is administered an AAV comprising a nucleic acid encoding a VH domain and an AAV comprising a nucleic acid encoding a VL domain. In other embodiments, a subject is administered an AAV comprising a nucleic acid encoding a VH domain and a VL domain. In certain embodiments, the VH and VL domains are over-expressed. [00458] Another approach to gene therapy involves transferring a gene to cells in tissue culture by such methods as electroporation, lipofection, calcium phosphate mediated transfection, or viral infection. Usually, the method of transfer includes the transfer of a selectable marker to the cells. The cells are then placed under selection to isolate those cells that have taken up and are expressing the transferred gene. Those cells are then delivered to a subject. [00459] In this embodiment, the nucleic acid is introduced into a cell prior to administration in vivo of the resulting recombinant cell. Such introduction can be carried out by any method known in the art, including but not limited to transfection, electroporation, microinjection, infection with a viral or bacteriophage vector containing the nucleic acid sequences, cell fusion, chromosome-mediated gene transfer, microcellmediated gene transfer, spheroplast fusion, etc. Numerous techniques are known in the art for the introduction of foreign genes into cells (see, e.g., Loeffler and Behr, 1993, Meth. Enzymol.217:599-618; Cohen et al., 1993, Meth. Enzymol.217:618-644; Clin. Pharma. Ther. 29:69-92 (1985)) and can be used in accordance with the methods provided herein, provided that the necessary developmental and physiological functions of the recipient cells are not disrupted. The technique should provide for the stable transfer of the nucleic acid to the cell, so that the nucleic acid is expressible by the cell, such as heritable and expressible by its cell progeny. [00460] The resulting recombinant cells can be delivered to a subject by various methods known in the art. Recombinant blood cells (e.g., hematopoietic stem or progenitor cells) can be administered intravenously. The amount of cells envisioned for use depends on the desired effect, patient state, etc., and can be determined by one skilled in the art. [00461] Cells into which a nucleic acid can be introduced for purposes of gene therapy encompass any desired, available cell type, and include but are not limited to epithelial cells, endothelial cells, keratinocytes, fibroblasts, muscle cells, hepatocytes; blood cells such as T lymphocytes, B lymphocytes, monocytes, macrophages, neutrophils, eosinophils, megakaryocytes, granulocytes; various stem or progenitor cells, in particular hematopoietic stem or progenitor cells, e.g., as obtained from bone marrow, umbilical cord blood, peripheral blood, fetal liver, etc. [00462] In a specific embodiment, the cell used for gene therapy is autologous to the subject. [00463] In an embodiment in which recombinant cells are used in gene therapy, nucleic acid sequences encoding an antibody are introduced into the cells such that they are expressible by the cells or their progeny, and the recombinant cells are then administered in vivo for therapeutic effect. In a specific embodiment, stem or progenitor cells are used. Any stem and/or progenitor cells which can be isolated and maintained in vitro can potentially be used in accordance with this embodiment of the methods provided herein (see e.g., PCT Publication WO 94/08598; Stemple and Anderson, 1992, Cell 71:973-985; Rheinwald, 1980, Meth. Cell Bio.21A:229; and Pittelkow and Scott, 1986, Mayo Clinic Proc.61:771). [00464] In a specific embodiment, the nucleic acid to be introduced for purposes of gene therapy comprises an inducible promoter operably linked to the coding region, such that expression of the nucleic acid is controllable by controlling the presence or absence of the appropriate inducer of transcription. Kits [00465] Also provided herein are kits comprising an antibody (e.g., an anti-IL-23R antibody) provided herein, or a composition (e.g., a pharmaceutical composition) thereof, packaged into suitable packaging material. A kit optionally includes a label or packaging insert including a description of the components or instructions for use in vitro, in vivo, or ex vivo, of the components therein. [00466] The term “packaging material” refers to a physical structure housing the components of the kit. The packaging material can maintain the components sterilely, and can be made of material commonly used for such purposes (e.g., paper, corrugated fiber, glass, plastic, foil, ampoules, vials, tubes, etc.). [00467] Kits provided herein can include labels or inserts. Labels or inserts include “printed matter,” e.g., paper or cardboard, separate or affixed to a component, a kit or packing material (e.g., a box), or attached to, for example, an ampoule, tube, or vial containing a kit component. Labels or inserts can additionally include a computer readable medium, such as a disk (e.g., hard disk, card, memory disk), optical disk such as CD- or DVD-ROM/RAM, DVD, MP3, magnetic tape, or an electrical storage media such as RAM and ROM or hybrids of these such as magnetic/optical storage media, FLASH media, or memory type cards. Labels or inserts can include information identifying manufacturer information, lot numbers, manufacturer location, and date. [00468] Kits provided herein can additionally include other components. Each component of the kit can be enclosed within an individual container, and all of the various containers can be within a single package. Kits can also be designed for cold storage. A kit can further be designed to contain antibodies provided herein, or cells that contain nucleic acids encoding the antibodies provided herein. The cells in the kit can be maintained under appropriate storage conditions until ready to use. [00469] Also provided herein are panels of antibodies that immunospecifically bind to an IL- 23R antigen. In specific embodiments, provided herein are panels of antibodies having different association rate constants, different dissociation rate constants, different affinities for IL-23R antigen, and/or different specificities for an IL-23R antigen. In certain embodiments, provided herein are panels of about 10, preferably about 25, about 50, about 75, about 100, about 125, about 150, about 175, about 200, about 250, about 300, about 350, about 400, about 450, about 500, about 550, about 600, about 650, about 700, about 750, about 800, about 850, about 900, about 950, or about 1000 antibodies or more. Panels of antibodies can be used, for example, in 96 well or 384 well plates, such as for assays such as ELISAs. [00470] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although methods and materials similar or equivalent to those described herein can be used in the practice or testing of the invention, suitable methods and materials are described herein. [00471] As used herein, numerical values are often presented in a range format throughout this document. The use of a range format is merely for convenience and brevity and should not be construed as an inflexible limitation on the scope of the invention unless the context clearly indicates otherwise. Accordingly, the use of a range expressly includes all possible subranges, all individual numerical values within that range, and all numerical values or numerical ranges including integers within such ranges and fractions of the values or the integers within ranges unless the context clearly indicates otherwise. This construction applies regardless of the breadth of the range and in all contexts throughout this patent document. Thus, for example, reference to a range of 90-100% includes 91-99%, 92-98%, 93-95%, 91-98%, 91-97%, 91-96%, 91-95%, 91-94%, 91-93%, and so forth. Reference to a range of 90-100% also includes 91%, 92%, 93%, 94%, 95%, 95%, 97%, etc., as well as 91.1%, 91.2%, 91.3%, 91.4%, 91.5%, etc., 92.1%, 92.2%, 92.3%, 92.4%, 92.5%, etc., and so forth. [00472] In addition, reference to a range of 1-3, 3-5, 5-10, 10-20, 20-30, 30-40, 40-50, 50-60, 60-70, 70-80, 80-90, 90-100, 100-110, 110-120, 120-130, 130-140, 140-150, 150-160, 160-170, 170- 180, 180-190, 190-200, 200-225, 225-250 includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, etc. In a further example, reference to a range of 25-250, 250-500, 500-1,000, 1,000- 2,500, 2,500-5,000, 5,000-25,000, 25,000-50,000 includes any numerical value or range within or encompassing such values, e.g., 25, 26, 27, 28, 29…250, 251, 252, 253, 254…500, 501, 502, 503, 504…, etc. [00473] As also used herein a series of ranges are disclosed throughout this document. The use of a series of ranges include combinations of the upper and lower ranges to provide another range. This construction applies regardless of the breadth of the range and in all contexts throughout this patent document. Thus, for example, reference to a series of ranges such as 5-10, 10-20, 20-30, 30- 40, 40-50, 50-75, 75-100, 100-150, includes ranges such as 5-20, 5-30, 5-40, 5-50, 5-75, 5-100, 5-150, and 10-30, 10-40, 10-50, 10-75, 10-100, 10-150, and 20-40, 20-50, 20-75, 20-100, 20-150, and so forth. [00474] For the sake of conciseness, certain abbreviations are used herein. One example is the single letter abbreviation to represent amino acid residues. The amino acids and their corresponding three letter and single letter abbreviations are as follows: [00475] The invention is generally disclosed herein using affirmative language to describe the numerous embodiments. The invention also specifically includes embodiments in which particular subject matter is excluded, in full or in part, such as substances or materials, method steps and conditions, protocols, procedures, assays or analysis. Thus, even though the invention is generally not expressed herein in terms of what the invention does not include, aspects that are not expressly included in the invention are nevertheless disclosed herein. ASPECTS OF THE PRESENT INVENTION [00476] The following aspects illustrate and are not intended to limit scope of the present invention. Instead, these aspects provide guidance to any skilled artisan on how to prepare and use compounds, compositions and methods taught by the present invention, where such skilled artisans will appreciate that modifications may be made without departing from the spirit and scope of the invention. 1. An isolated monoclonal antibody or antigen binding fragment thereof that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:236, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:237; b. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:798, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:799; c. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:792, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:793; d. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:786, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:787; e. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:138, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:139; f. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:144, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:145; g. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:152, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:153; h. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:154, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:155; i. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:156, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:157; j. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:160, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:161; k. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:164, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:165; l. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:166, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:167; m. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:168, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:169; n. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:174, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:175; o. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:788, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:789; p. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:186, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:187; q. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:828, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:829; r. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:790, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:791; s. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:188, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:189; t. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:884, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:885; u. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:192, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:193; v. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:194, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:195; w. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:198, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:199; x. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:200, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:201; y. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:202, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:203; z. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:204, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:205; aa. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:206, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:207; bb. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:216, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:217; cc. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:222, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:223; dd. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:230, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:231; ee. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:232, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:233; ff. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:234, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:235; gg. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:238, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:239; hh. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:246, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:247; ii. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:248, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:249; jj. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:254, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:255; kk. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:260, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:261; ll. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:262, and a LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:263; or mm. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:264, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:265. 2. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 1 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: nn. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:570, 571, and 572, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:573, 574, and 575, respectively; oo. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:936, 937, and 938, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; pp. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:918, 919, and 920, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:921, 922, and 923, respectively; qq. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:900, 901, and 902, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:903, 904, and 905, respectively; rr. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:276, 277, and 278, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:279, 280, and 281, respectively; ss. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:294, 295, and 296, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:297, 298, and 299, respectively; tt. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:318, 319, and 320, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:321, 322, and 323, respectively; uu. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:324, 325, and 326, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:327, 328, and 329, respectively; vv. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:330, 331, and 332, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:333, 334, and 335, respectively; ww. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:342, 343, and 344, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:345, 346, and 347, respectively; xx. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:354, 355, and 356, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:357, 358, and 359, respectively; yy. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:360, 361, and 362, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:363, 364, and 365, respectively; zz. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:366, 367, and 368, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:369, 370, and 371, respectively; aaa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:384, 385, and 386, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:387, 388, and 389, respectively; bbb. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:906, 907, and 908, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:909, 910, and 911, respectively; ccc. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:420, 421, and 422, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:423, 424, and 425, respectively; ddd. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1026, 1027, and 1028, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1029, 1030, and 1031, respectively; eee. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:912, 913, and 914, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:915, 916, and 917, respectively; fff. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:426, 427, and 428, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:429, 430, and 431, respectively; ggg. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1194, 1195, and 1196, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1197, 1198, and 1199, respectively; hhh. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:438, 439, and 440, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:441, 442, and 443, respectively; iii. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:444, 445, and 446, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:447, 448, and 449, respectively; jjj. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:456, 457, and 458, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:459, 460, and 461, respectively; kkk. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:462, 463, and 464, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:465, 466, and 467, respectively; lll. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:468, 469, and 470, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:471, 472, and 473, respectively; mmm. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:474, 475, and 476, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:477, 478, and 479, respectively; nnn. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:480, 481, and 482, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:483, 484, and 485, respectively; ooo. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:510, 511, and 512, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:513, 514, and 515, respectively; ppp. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:528, 529, and 530, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:531, 532, and 533, respectively; qqq. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:552, 553, and 554, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:555, 556, and 557, respectively; rrr. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:558, 559, and 560, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:561, 562, and 563, respectively; sss. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:564, 565, and 566, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:567, 568, and 569, respectively; ttt. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:576, 577, and 578, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:579, 580, and 581, respectively; uuu. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:600, 601, and 602, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:603, 604, and 605, respectively; vvv. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:606, 607, and 608, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:609, 610, and 611, respectively; www. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:624, 625, and 626, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:627, 628, and 629, respectively; xxx. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:642, 643, and 644, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:645, 646, and 647, respectively; yyy. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:648, 649, and 650, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:651, 652, and 653, respectively; or zzz. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:654, 655, and 656, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:657, 658, and 659, respectively. 3. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 1 or 2 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising the amino acid sequence of SEQ ID NO:236, and a VL comprising the amino acid sequence of SEQ ID NO:237; b. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; c. a VH comprising the amino acid sequence of SEQ ID NO:792, and a VL comprising the amino acid sequence of SEQ ID NO:793; d. a VH comprising the amino acid sequence of SEQ ID NO:786, and a VL comprising the amino acid sequence of SEQ ID NO:787; e. a VH comprising the amino acid sequence of SEQ ID NO:138, and a VL comprising the amino acid sequence of SEQ ID NO:139; f. a VH comprising the amino acid sequence of SEQ ID NO:144, and a VL comprising the amino acid sequence of SEQ ID NO:145; g. a VH comprising the amino acid sequence of SEQ ID NO:152, and a VL comprising the amino acid sequence of SEQ ID NO:153; h. a VH comprising the amino acid sequence of SEQ ID NO:154, and a VL comprising the amino acid sequence of SEQ ID NO:155; i. a VH comprising the amino acid sequence of SEQ ID NO:156, and a VL comprising the amino acid sequence of SEQ ID NO:157; j. a VH comprising the amino acid sequence of SEQ ID NO:160, and a VL comprising the amino acid sequence of SEQ ID NO:161; k. a VH comprising the amino acid sequence of SEQ ID NO:164, and a VL comprising the amino acid sequence of SEQ ID NO:165; l. a VH comprising the amino acid sequence of SEQ ID NO:166, and a VL comprising the amino acid sequence of SEQ ID NO:167; m. a VH comprising the amino acid sequence of SEQ ID NO:168, and a VL comprising the amino acid sequence of SEQ ID NO:169; n. a VH comprising the amino acid sequence of SEQ ID NO:174, and a VL comprising the amino acid sequence of SEQ ID NO:175; o. a VH comprising the amino acid sequence of SEQ ID NO:788, and a VL comprising the amino acid sequence of SEQ ID NO:789; p. a VH comprising the amino acid sequence of SEQ ID NO:186, and a VL comprising the amino acid sequence of SEQ ID NO:187; q. a VH comprising the amino acid sequence of SEQ ID NO:828, and a VL comprising the amino acid sequence of SEQ ID NO:829; r. a VH comprising the amino acid sequence of SEQ ID NO:790, and a VL comprising the amino acid sequence of SEQ ID NO:791; s. a VH comprising the amino acid sequence of SEQ ID NO:188, and a VL comprising the amino acid sequence of SEQ ID NO:189; t. a VH comprising the amino acid sequence of SEQ ID NO:884, and a VL comprising the amino acid sequence of SEQ ID NO:885; u. a VH comprising the amino acid sequence of SEQ ID NO:192, and a VL comprising the amino acid sequence of SEQ ID NO:193; v. a VH comprising the amino acid sequence of SEQ ID NO:194, and a VL comprising the amino acid sequence of SEQ ID NO:195; w. a VH comprising the amino acid sequence of SEQ ID NO:198, and a VL comprising the amino acid sequence of SEQ ID NO:199; x. a VH comprising the amino acid sequence of SEQ ID NO:200, and a VL comprising the amino acid sequence of SEQ ID NO:201; y. a VH comprising the amino acid sequence of SEQ ID NO:202, and a VL comprising the amino acid sequence of SEQ ID NO:203; z. a VH comprising the amino acid sequence of SEQ ID NO:204, and a VL comprising the amino acid sequence of SEQ ID NO:205; aa. a VH comprising the amino acid sequence of SEQ ID NO:206, and a VL comprising the amino acid sequence of SEQ ID NO:207; bb. a VH comprising the amino acid sequence of SEQ ID NO:216, and a VL comprising the amino acid sequence of SEQ ID NO:217; cc. a VH comprising the amino acid sequence of SEQ ID NO:222, and a VL comprising the amino acid sequence of SEQ ID NO:223; dd. a VH comprising the amino acid sequence of SEQ ID NO:230, and a VL comprising the amino acid sequence of SEQ ID NO:231; ee. a VH comprising the amino acid sequence of SEQ ID NO:232, and a VL comprising the amino acid sequence of SEQ ID NO:233; ff. a VH comprising the amino acid sequence of SEQ ID NO:234, and a VL comprising the amino acid sequence of SEQ ID NO:235; gg. a VH comprising the amino acid sequence of SEQ ID NO:238, and a VL comprising the amino acid sequence of SEQ ID NO:239; hh. a VH comprising the amino acid sequence of SEQ ID NO:246, and a VL comprising the amino acid sequence of SEQ ID NO:247; ii. a VH comprising the amino acid sequence of SEQ ID NO:248, and a VL comprising the amino acid sequence of SEQ ID NO:249; jj. a VH comprising the amino acid sequence of SEQ ID NO:254, and a VL comprising the amino acid sequence of SEQ ID NO:255; kk. a VH comprising the amino acid sequence of SEQ ID NO:260, and a VL comprising the amino acid sequence of SEQ ID NO:261; ll. a VH comprising the amino acid sequence of SEQ ID NO:262, and a VL comprising the amino acid sequence of SEQ ID NO:263; or mm. a VH comprising the amino acid sequence of SEQ ID NO:264, and a VL comprising the amino acid sequence of SEQ ID NO:265. 4. An isolated monoclonal antibody or active fragment thereof that binds human interleukin-23 receptor (IL-23R) on a mammalian cell of aspect 1, wherein the antibody or fragment comprises: a. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:786, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:787; b. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:790, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:791; c. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:792, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:793; d. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:798, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:799; or e. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:236, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:237. 5. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 2 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:570, 571, and 572, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:573, 574, and 575, respectively; b. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:936, 937, and 938, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; c. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:918, 919, and 920, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:921, 922, and 923, respectively; d. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:900, 901, and 902, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:903, 904, and 905, respectively; or e. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:912, 913, and 914, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:915, 916, and 917, respectively. 6. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 3 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising the amino acid sequence of SEQ ID NO:236, and a VL comprising the amino acid sequence of SEQ ID NO:237; b. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; c. a VH comprising the amino acid sequence of SEQ ID NO:792, and a VL comprising the amino acid sequence of SEQ ID NO:793; d. a VH comprising the amino acid sequence of SEQ ID NO:786, and a VL comprising the amino acid sequence of SEQ ID NO:787; or e. a VH comprising the amino acid sequence of SEQ ID NO:790, and a VL comprising the amino acid sequence of SEQ ID NO:791. 7. The isolated monoclonal antibody or antigen binding fragment thereof of any of aspects 1 to 6 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:918, 919, and 920, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:921, 922, and 923, respectively; b. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:936, 937, and 938, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; or c. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:570, 571, and 572, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:573, 574, and 575, respectively. 8. The isolated monoclonal antibody or antigen binding fragment thereof of any of aspects 1 to 7 that binds human interleukin-23 receptor (IL-23R) on a mammalian cell, wherein the antibody or fragment comprises: a. a VH comprising the amino acid sequence of SEQ ID NO:792, and a VL comprising the amino acid sequence of SEQ ID NO:793; b. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; or c. a VH comprising the amino acid sequence of SEQ ID NO:236, and a VL comprising the amino acid sequence of SEQ ID NO:237. 9. The isolated monoclonal antibody or antigen binding fragment thereof of any of aspects 1-8, wherein the mammalian cell is a human or rat cell. 10. The isolated monoclonal antibody or antigen binding fragment thereof of any of aspects 1-9, wherein the cell is a primary immune cell. 11. An isolated monoclonal antibody or antigen binding fragment thereof which recognizes human and rat interleukin-23 receptor (IL-23R), wherein the antibody or fragment comprises: a. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:202, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:203; b. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:252, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:253; c. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:156, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:157; d. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:798, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:799; e. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:150, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:151; f. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:204, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:205; g. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:884, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:885; h. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:188, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:189; or i. an HCDR1, and HCDR2 and an HCDR3 as set forth in SEQ ID NO:212, and an LCDR1, LCDR2 and LCDR3 set forth in SEQ ID NO:213. 12. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 11 which recognizes human and rat IL-23R, wherein the antibody or fragment comprises: a. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:468, 469, and 470 , respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:471, 472, and 473, respectively; b. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:618, 619, and 620, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:621, 622, and 623, respectively; c. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:330, 331, and 332, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:333, 334, and 335, respectively; d. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:936,937, and 938, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; e. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:312, 313, and 314, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:315, 316, and 317, respectively; f. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:474, 475, and 476, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:477, 478, and 479, respectively; g. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:1194, 1195, and 1196, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1197, 1198, and 1199, respectively; h. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:426, 427, and 428, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:429, 430, and 431, respectively; or i. a VH comprising an HCDR1, and HCDR2 and an HCDR3 having an amino acid sequence of SEQ ID NOs:498, 499, and 500, respectively and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:501, 502, and 503, respectively. 13. The isolated monoclonal antibody or antigen binding fragment thereof of any of aspects 11 or 12 which recognizes human and rat IL-23R, wherein the antibody or fragment comprises: a. a VH comprising the amino acid sequence of SEQ ID NO:202, and a VL comprising the amino acid sequence of SEQ ID NO:203; b. a VH comprising the amino acid sequence of SEQ ID NO:252, and a VL comprising the amino acid sequence of SEQ ID NO:253; c. a VH comprising the amino acid sequence of SEQ ID NO:156, and a VL comprising the amino acid sequence of SEQ ID NO:157; d. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; e. a VH comprising the amino acid sequence of SEQ ID NO:150, and a VL comprising the amino acid sequence of SEQ ID NO:151; f. a VH comprising the amino acid sequence of SEQ ID NO:204, and a VL comprising the amino acid sequence of SEQ ID NO:205; g. a VH comprising the amino acid sequence of SEQ ID NO:884, and a VL comprising the amino acid sequence of SEQ ID NO:885; h. a VH comprising the amino acid sequence of SEQ ID NO:188, and a VL comprising the amino acid sequence of SEQ ID NO:189; or i. a VH comprising the amino acid sequence of SEQ ID NO:212, and a VL comprising the amino acid sequence of SEQ ID NO:213. 14. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1252, an LCDR2 SEQ ID NO:1253, and an LCDR3 SEQ ID NO:1254 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:900, an HCDR2 SEQ ID NO:901 and an HCDR3 SEQ ID NO:902; b. an HCDR1 SEQ ID NO:906, an HCDR2 SEQ ID NO:907, and an HCDR3 SEQ ID NO:908; c. an HCDR1 SEQ ID NO:912, an HCDR2 SEQ ID NO:913, and an HCDR3 SEQ ID NO:914; d. an HCDR1 SEQ ID NO:918, an HCDR2 SEQ ID NO:919, and an HCDR3 SEQ ID NO:920; e. an HCDR1 SEQ ID NO:942, an HCDR2 SEQ ID NO:943, and an HCDR3 SEQ ID NO:944; f. an HCDR1 SEQ ID NO:948, an HCDR2 SEQ ID NO:949, and an HCDR3 SEQ ID NO:950; g. an HCDR1 SEQ ID NO:1014, an HCDR2 SEQ ID NO:1015, and an HCDR3 SEQ ID NO:1016; h. an HCDR1 SEQ ID NO:1026, an HCDR2 SEQ ID NO:1027, and an HCDR3 SEQ ID NO:1028; and i. an HCDR1 SEQ ID NO:1152, an HCDR2 SEQ ID NO:1153, and an HCDR3 SEQ ID NO:1154. 15. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 13 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1252, an LCDR2 SEQ ID NO:1253, and an LCDR3 SEQ ID NO:1254 or VL having the amino acid sequence SEQ ID NO:1247 and a VH sequence selected from SEQ ID NO:786, 788, 790, 792, 800, 802, 824, 828 and 870. 16. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1255, an LCDR2 SEQ ID NO:1256, and an LCDR3 SEQ ID NO:1257 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:924, an HCDR2 SEQ ID NO:925, and an HCDR3 SEQ ID NO:926; b. an HCDR1 SEQ ID NO:1002, an HCDR2 SEQ ID NO:1003, and an HCDR3 SEQ ID NO:1004; c. an HCDR1 SEQ ID NO:1032, an HCDR2 SEQ ID NO:1033, and an HCDR3 SEQ ID NO:1034; d. an HCDR1 SEQ ID NO:1044, an HCDR2 SEQ ID NO:1045, and an HCDR3 SEQ ID NO:1046; e. an HCDR1 SEQ ID NO:1050, an HCDR2 SEQ ID NO:1051, and an HCDR3 SEQ ID NO:1052; f. an HCDR1 SEQ ID NO:1056, an HCDR2 SEQ ID NO:1057, and an HCDR3 SEQ ID NO:1058; g. an HCDR1 SEQ ID NO:1062, an HCDR2 SEQ ID NO:1063, and an HCDR3 SEQ ID NO:1064; h. an HCDR1 SEQ ID NO:1068, an HCDR2 SEQ ID NO:1069, and an HCDR3 SEQ ID NO:1070; i. an HCDR1 SEQ ID NO:1080, an HCDR2 SEQ ID NO:1081, and an HCDR3 SEQ ID NO:1082; j. an HCDR1 SEQ ID NO:1092, an HCDR2 SEQ ID NO:1093, and an HCDR3 SEQ ID NO:1094; k. an HCDR1 SEQ ID NO:1098, an HCDR2 SEQ ID NO:1099, and an HCDR3 SEQ ID NO:1100; l. an HCDR1 SEQ ID NO:1110, an HCDR2 SEQ ID NO:1111, and an HCDR3 SEQ ID NO:1112; m. an HCDR1 SEQ ID NO:1122, an HCDR2 SEQ ID NO:1123, and an HCDR3 SEQ ID NO:1124; n. an HCDR1 SEQ ID NO:1140, an HCDR2 SEQ ID NO:1141, and an HCDR3 SEQ ID NO:1142; o. an HCDR1 SEQ ID NO:1146, an HCDR2 SEQ ID NO:1147, and an HCDR3 SEQ ID NO:1148; and p. an HCDR1 SEQ ID NO:1158, an HCDR2 SEQ ID NO:1159, and an HCDR3 SEQ ID NO:1160. 17. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 16 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1255, an LCDR2 SEQ ID NO:1256, and an LCDR3 SEQ ID NO:1257 or having the amino acid sequence SEQ ID NO:1248 and a VH sequence selected from SEQ ID NO:794, 820, 830, 834, 836, 838, 840, 842, 846, 850, 852, 856, 860, 866, 868 and 872. 18. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1258, an LCDR2 SEQ ID NO:1259, and an LCDR3 SEQ ID NO:1260 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:930, an HCDR2 SEQ ID NO:931, and an HCDR3 SEQ ID NO:932; and b. an HCDR1 SEQ ID NO:954, an HCDR2 SEQ ID NO:955, and an HCDR3 SEQ ID NO:956. 19. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 18 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1258, an LCDR2 SEQ ID NO:1259, and an LCDR3 SEQ ID NO:1260 or VL having the amino acid sequence SEQ ID NO:1249; and a VH sequence selected from SEQ ID NO:796 and 804. 20. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1261, an LCDR2 SEQ ID NO:1262, and an LCDR3 SEQ ID NO:1263 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:960, an HCDR2 SEQ ID NO:961, and an HCDR3 SEQ ID NO:962; and b. an HCDR1 SEQ ID NO:1182, an HCDR2 SEQ ID NO:1183, and an HCDR3 SEQ ID NO:1184. 21. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 20 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1261, an LCDR2 SEQ ID NO:1262, and an LCDR3 SEQ ID NO:1263 or having the amino acid sequence SEQ ID NO:1250 and a VH sequence selected from SEQ ID NO:806 and 880. 22. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1264, an LCDR2 SEQ ID NO:1265, and an LCDR3 SEQ ID NO:1266 and a VH comprising CDR sequences selected from: a. an HCDR1 SEQ ID NO:1008, an HCDR2 SEQ ID NO:1009, and an HCDR3 SEQ ID NO:1010; b. an HCDR1 SEQ ID NO:1020, an HCDR2 SEQ ID NO:1021, and an HCDR3 SEQ ID NO:1022; c. an HCDR1 SEQ ID NO:1038, an HCDR2 SEQ ID NO:1039, and an HCDR3 SEQ ID NO:1040; d. an HCDR1 SEQ ID NO:1074, an HCDR2 SEQ ID NO:1075, and an HCDR3 SEQ ID NO:1076; e. an HCDR1 SEQ ID NO:1086, an HCDR2 SEQ ID NO:1087, and an HCDR3 SEQ ID NO:1088; f. an HCDR1 SEQ ID NO:1104, an HCDR2 SEQ ID NO:1105, and an HCDR3 SEQ ID NO:1106; g. an HCDR1 SEQ ID NO:1128, an HCDR2 SEQ ID NO:1129, and an HCDR3 SEQ ID NO:1130; and h. an HCDR1 SEQ ID NO:1134, an HCDR2 SEQ ID NO:1135, and an HCDR3 SEQ ID NO:1136. 23. The isolated monoclonal antibody or antigen binding fragment thereof of aspect 22 comprising a VL comprising CDR sequences of an LCDR1 SEQ ID NO:1264, an LCDR2 SEQ ID NO:1265, and an LCDR3 SEQ ID NO:1266 or VL having the amino acid sequence SEQ ID NO:1251; and a VH sequence selected from SEQ ID NO: 806 and 880822, 826, 832, 844, 848, 854, 862 and 864. 24. A VHH antibody or nanobody that binds interleukin-23 receptor (IL-23R) comprising a VH sequence selected from SEQ ID NO:786, 788, 790, 792, 800, 802, 824, 828, 870, 794, 820, 830, 834, 836, 838, 840, 842, 846, 850, 852, 856, 860, 866, 868, 872, 796, 804, 806, 880, 822, 826, 832, 844, 848, 854, 862 and 864. 25. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising: a. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:138, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:139; b. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:142, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:143; c. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:144, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:145; d. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:148, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:149; e. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:150, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:151; f. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:152, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:153; g. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:154, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:155; h. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:156, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:157; i. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:158, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:159; j. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:160, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:161; k. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:162, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:163; l. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:164, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:165; m. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:166, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:167; n. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:168, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:169; o. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:170, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:171; p. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:172, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:173; q. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:174, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:175; r. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:176, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:177; s. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:178, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:179; t. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:180, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:181; u. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:182, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:183; v. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:186, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:187; w. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:188, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:189; x. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:190, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:191; y. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:192, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:193; z. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:194, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:195; aa. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:196, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:197; bb. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:198, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:199; cc. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:200, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:201; dd. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:202, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:203; ee. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:204, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:205; ff. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:206, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:207; gg. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:208, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:209; hh. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:210, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:211; ii. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:212, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:213; jj. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:214, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:215; kk. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:216, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:217; ll. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:218, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:219; mm. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:220, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:221; nn. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:222, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:223; oo. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:226, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:227; pp. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:228, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:229; qq. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:230, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:231; rr. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:232, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:233; ss. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:234, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:235; tt. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:236, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:237; uu. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:238, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:239; vv. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:240, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:241; ww. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:246, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:247; xx. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:248, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:249; yy. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:250, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:251; zz. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:252, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:253; aaa. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:254, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:255; bbb. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:256, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:257; ccc. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:258, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:259; ddd. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:260, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:261; eee. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:262, and a LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:263; fff. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:264, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:265; ggg. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:268, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:269; hhh. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:786, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:787; iii. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:788, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:789; jjj. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:790, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:791; kkk. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:792, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:793; lll. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:798, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:799; mmm. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:806, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:807; nnn. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:808, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:809; ooo. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:810, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:811; ppp. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:812, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:813; qqq. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:814, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:815; rrr. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:816, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:817; sss. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:818, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:819; ttt. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:820, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:821; uuu. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:822, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:823; vvv. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:824, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:825; www. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:826, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:827; xxx. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:828, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:829; yyy. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:830, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:831; zzz. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:832, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:833; aaaa. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:836, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:837; bbbb. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:838, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:839; cccc. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:840, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:841; dddd. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO: 842, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:843; eeee. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:846, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:847; ffff. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:848, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:849; gggg. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:850, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:851; hhhh. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:852, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:853; iiii. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:854, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:855; jjjj. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:856, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:857; kkkk. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:858, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:859; llll. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:860, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:861; mmmm. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:862, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:863; nnnn. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:864, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:865; oooo. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:866, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:867; pppp. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:868, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:869; qqqq. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:870, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:871; rrrr. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:872, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:873; ssss. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:874, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:875; tttt. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:876, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:877; uuuu. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:878, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:879; vvvv. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:880, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:881; wwww. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:882, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:883; xxxx. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:884, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:885; yyyy. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:886, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:887; zzzz. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:888, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:889; or aaaaa. an HCDR1, an HCDR2, and an HCDR3 as set forth in SEQ ID NO:890, and an LCDR1, an LCDR2, and an LCDR3 as set forth in SEQ ID NO:891. 26. An isolated monoclonal antibody or antigen binding fragment thereof that binds interleukin- 23 receptor (IL-23R) comprising: a. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:276, 277, and 278, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:279, 280, and 281, respectively; b. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:288, 289, and 290, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:291, 292, and 293, respectively; c. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:294, 295, and 296, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:297, 298, and 299, respectively; d. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:306, 307, and 308, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:309, 310, and 311, respectively; e. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:312, 313, and 314, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:315, 316, and 317, respectively; f. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:318, 319, and 320, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:321, 322, and 323, respectively; g. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:324, 325, and 326, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:327, 328, and 329, respectively; h. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:330, 331, and 332, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:333, 334, and 335, respectively; i. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:336, 337, and 338, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:339, 340, and 341, respectively; j. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:342, 343, and 344, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:345, 346, and 347, respectively; k. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:348, 349, and 350, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:351, 352, and 353, respectively; l. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:354, 355, and 356, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:357, 358, and 359, respectively; m. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:360, 361, and 362, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:363, 364, and 365, respectively; n. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:366, 367, and 368, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:369, 370, and 371, respectively; o. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:372, 373, and 374, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:375, 376, and 377, respectively; p. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:378, 379, and 380, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:381, 382, and 383, respectively; q. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:384, 385, and 386, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:387, 388, and 389, respectively; r. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:390, 391, and 392, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:393, 394, and 395, respectively; s. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:396, 397, and 398, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:399, 400, and 401, respectively; t. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:402, 403, and 404, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:405, 406, and 407, respectively; u. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:408, 409, and 410, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:411, 412, and 413, respectively; v. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:420, 421, and 422, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:423, 424, and 425, respectively; w. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:426, 427, and 428, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:429, 430, and 431, respectively; x. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:432, 433, and 434, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:435, 436, and 437, respectively; y. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:438, 439, and 440, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:441, 442, and 443, respectively; z. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:444, 445, and 446, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:447, 448, and 449, respectively; aa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:450, 451, and 452, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:453, 454, and 455, respectively; bb. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:456, 457, and 458, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:459, 460, and 461, respectively; cc. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:462, 463, and 464, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:465, 466, and 467, respectively; dd. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:468, 469, and 470, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:471, 472, and 473, respectively; ee. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:474, 475, and 476, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:477, 478, and 479, respectively; ff. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:480, 481, and 482, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:483, 484, and 485, respectively; gg. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:486, 487, and 488, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:489, 490, and 491, respectively; hh. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:492, 493, and 494, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:495, 496, and 497, respectively; ii. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:498, 499, and 500, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:501, 502, and 503, respectively; jj. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:504, 505, and 506, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:507, 508, and 509, respectively; kk. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:510, 511, and 512, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:513, 514, and 515, respectively; ll. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:516, 517, and 518, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:519, 520, and 521, respectively; mm. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:522, 523, and 524, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:525, 526, and 527, respectively; nn. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:528, 529, and 530, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:531, 532, and 533, respectively; oo. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:540, 541, and 542, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:543, 544, and 545, respectively; pp. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:546, 547, and 548, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:549, 550, and 551, respectively; qq. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:552, 553, and 554, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:555, 556, and 557, respectively; rr. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:558, 559, and 560, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:561, 562, and 563, respectively; ss. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:564, 565, and 566, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:567, 568, and 569, respectively; tt. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:570, 571, and 572, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:573, 574, and 575, respectively; uu. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:576, 577, and 578, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:579, 580, and 581, respectively; vv. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:582, 583, and 584, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:585, 586, and 587, respectively; ww. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:600, 601, and 602, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:603, 604, and 605, respectively; xx. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:606, 607, and 608, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:609, 610, and 611, respectively; yy. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:612, 613, and 614, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:615, 616, and 617, respectively; zz. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:618, 619, and 620, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:621, 622, and 623, respectively; aaa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:624, 625, and 626, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:627, 628, and 629, respectively; bbb. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:630, 631, and 632, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:633, 634, and 635, respectively; ccc. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:636, 637, and 638, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:639, 640, and 641, respectively; ddd. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:642, 643, and 644, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:645, 646, and 647, respectively; eee. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:648, 649, and 650, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:651, 652, and 653, respectively; fff. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:654, 655, and 656, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:657, 658, and 659, respectively; ggg. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:666, 667, and 668, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:669, 670, and 671, respectively; hhh. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:900, 901, and 902, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:903, 904, and 905, respectively; iii. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:906, 907, and 908, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:909, 910, and 911, respectively; jjj. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:912, 913, and 914, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:915, 916, and 917, respectively; kkk. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:918, 919, and 920, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:921, 922, and 923, respectively; lll. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:936, 937, and 938, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:939, 940, and 941, respectively; mmm. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:960, 961, and 962, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:963, 964, and 965, respectively; nnn. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:966, 967, and 968, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:969, 970, and 971, respectively; ooo. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:972, 973, and 974, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:975, 976, and 977, respectively; ppp. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:978, 979, and 980, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:981, 982, and 983, respectively; qqq. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:984, 985, and 986, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:987, 988, and 989, respectively; rrr. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:990, 991, and 992, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:993, 994, and 995, respectively; sss. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:996, 997, and 998, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:999, 1000, and 1001, respectively; ttt. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1002, 1003, and 1004, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1005, 1006, and 1007, respectively; uuu. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1008, 1009, and 1010, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1011, 1012, and 1013, respectively; vvv. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1014, 1015, and 1016, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1017, 1018, and 1019, respectively; www. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1020, 1021, and 1022, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1023, 1024, and 1025, respectively; xxx. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1026, 1027, and 1028, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1029, 1030, and 1031, respectively; yyy. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1032, 1033, and 1034, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1035, 1036, and 1037, respectively; zzz. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1038, 1039, and 1040, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1041, 1042, and 1043, respectively; aaaa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1050, 1051, and 1052, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1053, 1054, and 1055, respectively; bbbb. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1056, 1057, and 1058, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1059, 1060, and 1061, respectively; cccc. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1062, 1063, and 1064, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1065, 1066, and 1067, respectively; dddd. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1068, 1069, and 1070, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1071, 1072, and 1073, respectively; eeee. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1080, 1081, and 1082, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1083, 1084, and 1085, respectively; ffff. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1086, 1087, and 1088, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1089, 1090, and 1091, respectively; gggg. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1092, 1093, and 1094, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1095, 1096, and 1097, respectively; hhhh. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1098, 1099, and 1100, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1101, 1102, and 1103, respectively; iiii. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1104, 1105, and 1106, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1107, 1108, and 1109, respectively; jjjj. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1110, 1111, and 1112, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1113, 1114, and 1115, respectively; kkkk. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1116, 1117, and 1118, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1119, 1120, and 1121, respectively; llll. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1122, 1123, and 1124, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1125, 1126, and 1127, respectively; mmmm. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1128, 1129, and 1130, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1131, 1132, and 1133, respectively; nnnn. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1134, 1135, and 1136, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1137, 1138, and 1139, respectively; oooo. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1140, 1141, and 1142, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1143, 1144, and 1145, respectively; pppp. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1146, 1147, and 1148, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1149, 1150, and 1151, respectively; qqqq. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1152, 1153, and 1154, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1155, 1156, and 1157, respectively; rrrr. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1158, 1159, and 1160, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1161, 1162, and 1163, respectively; ssss. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1164, 1165, and 1166, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1167, 1168, and 1169, respectively; tttt. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1170, 1171, and 1172, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1173, 1174, and 1175, respectively; uuuu. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1176, 1177, and 1178, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1179, 1180, and 1181, respectively; vvvv. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1182, 1183, and 1184, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1185, 1186, and 1187, respectively; wwww. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1188, 1189, and 1190, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1191, 1192, and 1193, respectively; xxxx. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1194, 1195, and 1196, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1197, 1198, and 1199, respectively; yyyy. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1200, 1201, and 1202, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1203, 1204, and 1205, respectively; zzzz. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1206, 1207, and 1208, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1209, 1210, and 1211, respectively; or aaaaa. a VH comprising an HCDR1, an HCDR2, and an HCDR3 having an amino acid sequence of SEQ ID NOs:1212, 1213, and 1214, respectively, and a VL comprising an LCDR1, an LCDR2, and an LCDR3 having an amino acid sequence of SEQ ID NOs:1215, 1216, and 1217, respectively. 27. The isolated monoclonal antibody or antigen binding fragment thereof of any of aspects 25 or 26 comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:138, and a VL comprising the amino acid sequence of SEQ ID NO:139; b. a VH comprising the amino acid sequence of SEQ ID NO:142, and a VL comprising the amino acid sequence of SEQ ID NO:143; c. a VH comprising the amino acid sequence of SEQ ID NO:144, and a VL comprising the amino acid sequence of SEQ ID NO:145; d. a VH comprising the amino acid sequence of SEQ ID NO:148, and a VL comprising the amino acid sequence of SEQ ID NO:149; e. a VH comprising the amino acid sequence of SEQ ID NO:150, and a VL comprising the amino acid sequence of SEQ ID NO:151; f. a VH comprising the amino acid sequence of SEQ ID NO:152, and a VL comprising the amino acid sequence of SEQ ID NO:153; g. a VH comprising the amino acid sequence of SEQ ID NO:154, and a VL comprising the amino acid sequence of SEQ ID NO:155; h. a VH comprising the amino acid sequence of SEQ ID NO:156, and a VL comprising the amino acid sequence of SEQ ID NO:157; i. a VH comprising the amino acid sequence of SEQ ID NO:158, and a VL comprising the amino acid sequence of SEQ ID NO:159; j. a VH comprising the amino acid sequence of SEQ ID NO:160, and a VL comprising the amino acid sequence of SEQ ID NO:161; k. a VH comprising the amino acid sequence of SEQ ID NO:162, and a VL comprising the amino acid sequence of SEQ ID NO:163; l. a VH comprising the amino acid sequence of SEQ ID NO:164, and a VL comprising the amino acid sequence of SEQ ID NO:165; m. a VH comprising the amino acid sequence of SEQ ID NO:166, and a VL comprising the amino acid sequence of SEQ ID NO:167; n. a VH comprising the amino acid sequence of SEQ ID NO:168, and a VL comprising the amino acid sequence of SEQ ID NO:169; o. a VH comprising the amino acid sequence of SEQ ID NO:170, and a VL comprising the amino acid sequence of SEQ ID NO:171; p. a VH comprising the amino acid sequence of SEQ ID NO:172, and a VL comprising the amino acid sequence of SEQ ID NO:173; q. a VH comprising the amino acid sequence of SEQ ID NO:174, and a VL comprising the amino acid sequence of SEQ ID NO:175; r. a VH comprising the amino acid sequence of SEQ ID NO:176, and a VL comprising the amino acid sequence of SEQ ID NO:177; s. a VH comprising the amino acid sequence of SEQ ID NO:178, and a VL comprising the amino acid sequence of SEQ ID NO:179; t. a VH comprising the amino acid sequence of SEQ ID NO:180, and a VL comprising the amino acid sequence of SEQ ID NO:181; u. a VH comprising the amino acid sequence of SEQ ID NO:182, and a VL comprising the amino acid sequence of SEQ ID NO:183; v. a VH comprising the amino acid sequence of SEQ ID NO:186, and a VL comprising the amino acid sequence of SEQ ID NO:187; w. a VH comprising the amino acid sequence of SEQ ID NO:188, and a VL comprising the amino acid sequence of SEQ ID NO:189; x. a VH comprising the amino acid sequence of SEQ ID NO:190, and a VL comprising the amino acid sequence of SEQ ID NO:191; y. a VH comprising the amino acid sequence of SEQ ID NO:192, and a VL comprising the amino acid sequence of SEQ ID NO:193; z. a VH comprising the amino acid sequence of SEQ ID NO:194, and a VL comprising the amino acid sequence of SEQ ID NO:195; aa. a VH comprising the amino acid sequence of SEQ ID NO:196, and a VL comprising the amino acid sequence of SEQ ID NO:197; bb. a VH comprising the amino acid sequence of SEQ ID NO:198, and a VL comprising the amino acid sequence of SEQ ID NO:199; cc. a VH comprising the amino acid sequence of SEQ ID NO:200, and a VL comprising the amino acid sequence of SEQ ID NO:201; dd. a VH comprising the amino acid sequence of SEQ ID NO:202, and a VL comprising the amino acid sequence of SEQ ID NO:203; ee. a VH comprising the amino acid sequence of SEQ ID NO:204, and a VL comprising the amino acid sequence of SEQ ID NO:205; ff. a VH comprising the amino acid sequence of SEQ ID NO:206, and a VL comprising the amino acid sequence of SEQ ID NO:207; gg. a VH comprising the amino acid sequence of SEQ ID NO:208, and a VL comprising the amino acid sequence of SEQ ID NO:209; hh. a VH comprising the amino acid sequence of SEQ ID NO:210, and a VL comprising the amino acid sequence of SEQ ID NO:211; ii. a VH comprising the amino acid sequence of SEQ ID NO:212, and a VL comprising the amino acid sequence of SEQ ID NO:213; jj. a VH comprising the amino acid sequence of SEQ ID NO:214, and a VL comprising the amino acid sequence of SEQ ID NO:215; kk. a VH comprising the amino acid sequence of SEQ ID NO:216, and a VL comprising the amino acid sequence of SEQ ID NO:217; ll. a VH comprising the amino acid sequence of SEQ ID NO:218, and a VL comprising the amino acid sequence of SEQ ID NO:219; mm. a VH comprising the amino acid sequence of SEQ ID NO:220, and a VL comprising the amino acid sequence of SEQ ID NO:221; nn. a VH comprising the amino acid sequence of SEQ ID NO:222, and a VL comprising the amino acid sequence of SEQ ID NO:223; oo. a VH comprising the amino acid sequence of SEQ ID NO:226, and a VL comprising the amino acid sequence of SEQ ID NO:227; pp. a VH comprising the amino acid sequence of SEQ ID NO:228, and a VL comprising the amino acid sequence of SEQ ID NO:229; qq. a VH comprising the amino acid sequence of SEQ ID NO:230, and a VL comprising the amino acid sequence of SEQ ID NO:231; rr. a VH comprising the amino acid sequence of SEQ ID NO:232, and a VL comprising the amino acid sequence of SEQ ID NO:233; ss. a VH comprising the amino acid sequence of SEQ ID NO:234, and a VL comprising the amino acid sequence of SEQ ID NO:235; tt. a VH comprising the amino acid sequence of SEQ ID NO:236, and a VL comprising the amino acid sequence of SEQ ID NO:237; uu. a VH comprising the amino acid sequence of SEQ ID NO:238, and a VL comprising the amino acid sequence of SEQ ID NO:239; vv. a VH comprising the amino acid sequence of SEQ ID NO:240, and a VL comprising the amino acid sequence of SEQ ID NO:241; ww. a VH comprising the amino acid sequence of SEQ ID NO:246, and a VL comprising the amino acid sequence of SEQ ID NO:247; xx. a VH comprising the amino acid sequence of SEQ ID NO:248, and a VL comprising the amino acid sequence of SEQ ID NO:249; yy. a VH comprising the amino acid sequence of SEQ ID NO:250, and a VL comprising the amino acid sequence of SEQ ID NO:251; zz. a VH comprising the amino acid sequence of SEQ ID NO:252, and a VL comprising the amino acid sequence of SEQ ID NO:253; aaa. a VH comprising the amino acid sequence of SEQ ID NO:254, and a VL comprising the amino acid sequence of SEQ ID NO:255; bbb. a VH comprising the amino acid sequence of SEQ ID NO:256, and a VL comprising the amino acid sequence of SEQ ID NO:257; ccc. a VH comprising the amino acid sequence of SEQ ID NO:258, and a VL comprising the amino acid sequence of SEQ ID NO:259; ddd. a VH comprising the amino acid sequence of SEQ ID NO:260, and a VL comprising the amino acid sequence of SEQ ID NO:261; eee. a VH comprising the amino acid sequence of SEQ ID NO:262, and a VL comprising the amino acid sequence of SEQ ID NO:263; fff. a VH comprising the amino acid sequence of SEQ ID NO:264, and a VL comprising the amino acid sequence of SEQ ID NO:265; ggg. a VH comprising the amino acid sequence of SEQ ID NO:268, and a VL comprising the amino acid sequence of SEQ ID NO:269; hhh. a VH comprising the amino acid sequence of SEQ ID NO:786, and a VL comprising the amino acid sequence of SEQ ID NO:787; iii. a VH comprising the amino acid sequence of SEQ ID NO:788, and a VL comprising the amino acid sequence of SEQ ID NO:789; jjj. a VH comprising the amino acid sequence of SEQ ID NO:790, and a VL comprising the amino acid sequence of SEQ ID NO:791; kkk. a VH comprising the amino acid sequence of SEQ ID NO:792, and a VL comprising the amino acid sequence of SEQ ID NO:793; lll. a VH comprising the amino acid sequence of SEQ ID NO:798, and a VL comprising the amino acid sequence of SEQ ID NO:799; mmm. a VH comprising the amino acid sequence of SEQ ID NO:806, and a VL comprising the amino acid sequence of SEQ ID NO:807; nnn. a VH comprising the amino acid sequence of SEQ ID NO:808, and a VL comprising the amino acid sequence of SEQ ID NO:809; ooo. a VH comprising the amino acid sequence of SEQ ID NO:810, and a VL comprising the amino acid sequence of SEQ ID NO:811; ppp. a VH comprising the amino acid sequence of SEQ ID NO:812, and a VL comprising the amino acid sequence of SEQ ID NO:813; qqq. a VH comprising the amino acid sequence of SEQ ID NO:814, and a VL comprising the amino acid sequence of SEQ ID NO:815; rrr. a VH comprising the amino acid sequence of SEQ ID NO:816, and a VL comprising the amino acid sequence of SEQ ID NO:817; sss. a VH comprising the amino acid sequence of SEQ ID NO:818, and a VL comprising the amino acid sequence of SEQ ID NO:819; ttt. a VH comprising the amino acid sequence of SEQ ID NO:820, and a VL comprising the amino acid sequence of SEQ ID NO:821; uuu. a VH comprising the amino acid sequence of SEQ ID NO:822, and a VL comprising the amino acid sequence of SEQ ID NO:823; vvv. a VH comprising the amino acid sequence of SEQ ID NO:824, and a VL comprising the amino acid sequence of SEQ ID NO:825; www. a VH comprising the amino acid sequence of SEQ ID NO:826, and a VL comprising the amino acid sequence of SEQ ID NO:827; xxx. a VH comprising the amino acid sequence of SEQ ID NO:828, and a VL comprising the amino acid sequence of SEQ ID NO:829; yyy. a VH comprising the amino acid sequence of SEQ ID NO:830, and a VL comprising the amino acid sequence of SEQ ID NO:831; zzz. a VH comprising the amino acid sequence of SEQ ID NO:832, and a VL comprising the amino acid sequence of SEQ ID NO:833; aaaa. a VH comprising the amino acid sequence of SEQ ID NO:836, and a VL comprising the amino acid sequence of SEQ ID NO:837; bbbb. a VH comprising the amino acid sequence of SEQ ID NO:838, and a VL comprising the amino acid sequence of SEQ ID NO:839; cccc. a VH comprising the amino acid sequence of SEQ ID NO:840, and a VL comprising the amino acid sequence of SEQ ID NO:841; dddd. a VH comprising the amino acid sequence of SEQ ID NO: 842, and a VL comprising the amino acid sequence of SEQ ID NO:843; eeee. a VH comprising the amino acid sequence of SEQ ID NO:846, and a VL comprising the amino acid sequence of SEQ ID NO:847; ffff. a VH comprising the amino acid sequence of SEQ ID NO:848, and a VL comprising the amino acid sequence of SEQ ID NO:849; gggg. a VH comprising the amino acid sequence of SEQ ID NO:850, and a VL comprising the amino acid sequence of SEQ ID NO:851; hhhh. a VH comprising the amino acid sequence of SEQ ID NO:852, and a VL comprising the amino acid sequence of SEQ ID NO:853; iiii. a VH comprising the amino acid sequence of SEQ ID NO:854, and a VL comprising the amino acid sequence of SEQ ID NO:855; jjjj. a VH comprising the amino acid sequence of SEQ ID NO:856, and a VL comprising the amino acid sequence of SEQ ID NO:857; kkkk. a VH comprising the amino acid sequence of SEQ ID NO:858, and a VL comprising the amino acid sequence of SEQ ID NO:859; llll. a VH comprising the amino acid sequence of SEQ ID NO:860, and a VL comprising the amino acid sequence of SEQ ID NO:861; mmmm. a VH comprising the amino acid sequence of SEQ ID NO:862, and a VL comprising the amino acid sequence of SEQ ID NO:863; nnnn. a VH comprising the amino acid sequence of SEQ ID NO:864, and a VL comprising the amino acid sequence of SEQ ID NO:865; oooo. a VH comprising the amino acid sequence of SEQ ID NO:866, and a VL comprising the amino acid sequence of SEQ ID NO:867; pppp. a VH comprising the amino acid sequence of SEQ ID NO:868, and a VL comprising the amino acid sequence of SEQ ID NO:869; qqqq. a VH comprising the amino acid sequence of SEQ ID NO:870, and a VL comprising the amino acid sequence of SEQ ID NO:871; rrrr. a VH comprising the amino acid sequence of SEQ ID NO:872, and a VL comprising the amino acid sequence of SEQ ID NO:873; ssss. a VH comprising the amino acid sequence of SEQ ID NO:874, and a VL comprising the amino acid sequence of SEQ ID NO:875; tttt. a VH comprising the amino acid sequence of SEQ ID NO:876, and a VL comprising the amino acid sequence of SEQ ID NO:877; uuuu. a VH comprising the amino acid sequence of SEQ ID NO:878, and a VL comprising the amino acid sequence of SEQ ID NO:879; vvvv. a VH comprising the amino acid sequence of SEQ ID NO:880, and a VL comprising the amino acid sequence of SEQ ID NO:881; wwww. a VH comprising the amino acid sequence of SEQ ID NO:882, and a VL comprising the amino acid sequence of SEQ ID NO:883; xxxx. a VH comprising the amino acid sequence of SEQ ID NO:884, and a VL comprising the amino acid sequence of SEQ ID NO:885; yyyy. a VH comprising the amino acid sequence of SEQ ID NO:886, and a VL comprising the amino acid sequence of SEQ ID NO:887; zzzz. a VH comprising the amino acid sequence of SEQ ID NO:888, and a VL comprising the amino acid sequence of SEQ ID NO:889; or aaaaa. a VH comprising the amino acid sequence of SEQ ID NO:890, and a VL comprising the amino acid sequence of SEQ ID NO:891. 28. The antibody or fragment of any of aspects 1-27, wherein the antibody is an IgG. 29. The antibody or fragment of any of aspects 1-28, wherein the antibody is a humanized or chimeric antibody or fragment thereof. 30. The isolated antibody or fragment of any of aspects 1-28 which is an antibody or fragment thereof wherein said isolated antibody is the form of an antibody F(ab')2, scFv fragment, domain antibody, minibody, diabody, triabody or tetrabody. 31. The antibody of any of aspects 1-30, wherein the antibody is genetically fused or chemically conjugated to an agent, wherein optionally the agent a detectable substance or is a drug, wherein optionally the detectable substance is selected from enzymes, prosthetic groups, fluorescent materials, luminescent materials, bioluminescent materials or chemiluminescent materials, wherein optionally the enzymes are selected from horseradish peroxidase, alkaline phosphatase, beta-galactosidase, or acetylcholinesterase; wherein optionally the prosthetic groups are selected from streptavidin/biotin or avidin/biotin; wherein optionally the fluorescent materials are selected from umbelliferone, fluorescein, fluorescein isothiocynate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride, or phycoerythrin; wherein optionally the luminescent material is luminol; wherein optionally the bioluminescent materials are selected from luciferase, luciferin, or aequorin; and wherein optionally the chemiluminescent materials are selected from 225Acγ-emitting, Auger-emitting, β-emitting, an alpha-emitting or positron-emitting radioactive isotope. 32. A nucleic acid molecule encoding the antibody of any of aspects 1-30 or a variable region or antigen binding fragment thereof. 33. A vector comprising the nucleic acid molecule of aspect 32. 34. A host cell transformed with the vector of aspect 33. 35. A composition comprising the antibody of any of aspects 1-31, the nucleic acid molecule of claim 30, or the vector of claim 31, and a pharmaceutically acceptable excipient. 36. A kit comprising the antibody of any of aspects 1-31. 37. A method for detecting, selecting and/or enriching interleukin-23 receptor (IL-23R) in a sample comprising contacting the sample with the antibody of any of aspects 1 to 31, wherein optionally the method comprising using the antibody of any of aspects 1 to 31 in an immunohistochemistry (IHC) assay, an immunocytochemistry (ICC) assay, an immunoblotting assay, an immunoprecipitation assay, a flow cytometry assay, an ELISA, a radioimmunoassay, a mass spectrometry assay, or high throughput screening assay; wherein: optionally the flow cytometry assay comprises three-steps of staining: (1) first, incubating the sample with the antibody of any of aspects 1 to 31; (2) second, incubating the sample with biotinylated anti-mouse IgG2a; (3) third, incubating the sample with streptavidin-PE; and wherein optionally, to establish the background for the flow cytometry assay, cells incubated with buffer alone or the negative control antibody are used as a control group in step (1), and cells incubated without the biotinylated anti-mouse IgG2a secondary reagent are used as an additional control group in step (2). 38. A method for detecting, selecting and/or enriching interleukin-23 receptor (IL-23R) in a sample comprising contacting the sample with an antibody that binds to the same epitope as the antibody of any of aspects 1 to 31, or an antibody that binds IL-23R competitively with the antibody of any of aspects 1 to 31. 39. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:202 and a VL comprising the amino acid sequence of SEQ ID NO:203; b. a VH comprising the amino acid sequence of SEQ ID NO:252 and a VL comprising the amino acid sequence of SEQ ID NO:253; or c. a VH comprising the amino acid sequence of SEQ ID NO:156 and a VL comprising the amino acid sequence of SEQ ID NO:157. 40. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:192 and a VL comprising the amino acid sequence of SEQ ID NO:193; b. a VH comprising the amino acid sequence of SEQ ID NO:194 and a VL comprising the amino acid sequence of SEQ ID NO:195; c. a VH comprising the amino acid sequence of SEQ ID NO:200 and a VL comprising the amino acid sequence of SEQ ID NO:201; d. a VH comprising the amino acid sequence of SEQ ID NO:218 and a VL comprising the amino acid sequence of SEQ ID NO:219; e. a VH comprising the amino acid sequence of SEQ ID NO:222 and a VL comprising the amino acid sequence of SEQ ID NO:223; f. a VH comprising the amino acid sequence of SEQ ID NO:260 and a VL comprising the amino acid sequence of SEQ ID NO:261; g. a VH comprising the amino acid sequence of SEQ ID NO:264 and a VL comprising the amino acid sequence of SEQ ID NO:265; h. a VH comprising the amino acid sequence of SEQ ID NO:154 and a VL comprising the amino acid sequence of SEQ ID NO:155; i. a VH comprising the amino acid sequence of SEQ ID NO:160 and a VL comprising the amino acid sequence of SEQ ID NO:161; or j. a VH comprising the amino acid sequence of SEQ ID NO:164 and a VL comprising the amino acid sequence of SEQ ID NO:165. 41. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:786 and a VL comprising the amino acid sequence of SEQ ID NO:787; b. a VH comprising the amino acid sequence of SEQ ID NO:790 and a VL comprising the amino acid sequence of SEQ ID NO:791; c. a VH comprising the amino acid sequence of SEQ ID NO:792 and a VL comprising the amino acid sequence of SEQ ID NO:793; d. a VH comprising the amino acid sequence of SEQ ID NO:236 and a VL comprising the amino acid sequence of SEQ ID NO:237; e. a VH comprising the amino acid sequence of SEQ ID NO:826 and a VL comprising the amino acid sequence of SEQ ID NO:827; or f. a VH comprising the amino acid sequence of SEQ ID NO:828 and a VL comprising the amino acid sequence of SEQ ID NO:829. 42. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:196 and a VL comprising the amino acid sequence of SEQ ID NO:197; b. a VH comprising the amino acid sequence of SEQ ID NO:262 and a VL comprising the amino acid sequence of SEQ ID NO:263; or c. a VH comprising the amino acid sequence of SEQ ID NO:152 and a VL comprising the amino acid sequence of SEQ ID NO:153. 43. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:798 and a VL comprising the amino acid sequence of SEQ ID NO:799. 44. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:206 and a VL comprising the amino acid sequence of SEQ ID NO:207; b. a VH comprising the amino acid sequence of SEQ ID NO:250 and a VL comprising the amino acid sequence of SEQ ID NO:251; c. a VH comprising the amino acid sequence of SEQ ID NO:144 and a VL comprising the amino acid sequence of SEQ ID NO:145; or d. a VH comprising the amino acid sequence of SEQ ID NO:170 and a VL comprising the amino acid sequence of SEQ ID NO:171. 45. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:150 and a VL comprising the amino acid sequence of SEQ ID NO:151. 46. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:198 and a VL comprising the amino acid sequence of SEQ ID NO:199; or b. a VH comprising the amino acid sequence of SEQ ID NO:240 and a VL comprising the amino acid sequence of SEQ ID NO:241. 47. The method of aspect 38, comprising contacting the sample with an antibody that binds to the same epitope and/or binds IL-23R competitively with the antibody comprising: a. a VH comprising the amino acid sequence of SEQ ID NO:204 and a VL comprising the amino acid sequence of SEQ ID NO:205; or b. a VH comprising the amino acid sequence of SEQ ID NO:884 and a VL comprising the amino acid sequence of SEQ ID NO:885. 48. The method of any of aspects 37 to 47, wherein the method is for detecting, selecting and/or enriching human IL-23R. 49. The method of any of aspects 37 to 47, wherein the method is for detecting, selecting and/or enriching cells that express IL-23R. 50. The method of any of aspects 37 to 47, wherein the method is for detecting denatured IL-23R. 51. The method of any of aspects 37 to 47, wherein the method comprising contacting the sample with two or more antibodies each being the antibody of any of aspects1 to 29. 52. The method of aspect 49, wherein the two or more antibodies bind to different epitopes of IL- 23R. 53. The method of any of aspects 37 to 52, wherein the sample is from a human subject. 54. The method of aspect 53, wherein the human subject has a disease or disorder. 55. The method of aspect 54, wherein the disease or disorder is an IL-23R associated disease or disorder. 56. The method of aspect 53, wherein the human subject is a healthy human subject. 57. A method of antagonizing or inhibiting IL-23R in a cell comprising contacting the cell with the antibody of any of aspects 1 to 31. 58. A method of treating a disease or disorder in a subject, comprising administering to the subject the composition of aspect 35 or the antibody of any of aspects 1 to 31. 59. The method of aspect 58, wherein the disease or disorder is an IL-23R associated disease or disorder. 60. The method according to aspect 58, wherein the disease or disorder is associated with inflammatory, autoimmune inflammation diseases and/or related disorders. 61. The method according to aspect 60, wherein the disease or disorder associated with inflammatory, autoimmune inflammation diseases and/or related disorders is selected from multiple sclerosis, asthma, rheumatoid arthritis, inflammation of the gut, inflammatory bowel diseases (IBDs), juvenile IBD, adolescent IBD, Crohn’s disease, ulcerative colitis, Celiac disease (nontropical Sprue), microscopic colitis, collagenous colitis, eosinophilic gastroenteritis/esophagitis, colitis associated with radio- or chemo-therapy, colitis associated with disorders of innate immunity as in leukocyte adhesion deficiency-1, sarcoidosis, Systemic Lupus Erythematosus, ankylosing spondylitis (axial spondyloarthritis), psoriatic arthritis, psoriasis (e.g., plaque psoriasis, guttate psoriasis, inverse psoriasis, pustular psoriasis, Palmo-Plantar Pustulosis, psoriasis vulgaris, or erythrodermic psoriasis), atopic dermatitis, acne ectopica, enteropathy associated with seronegative arthropathies, chronic granulomatous disease, glycogen storage disease type 1b, Hermansky-Pudlak syndrome, Chediak- Higashi syndrome, Wiskott-Aldrich Syndrome, pouchitis, pouchitis resulting after proctocolectomy and ileoanal anastomosis, gastrointestinal cancer, pancreatitis, insulin-dependent diabetes mellitus, mastitis, cholecystitis, cholangitis, primary biliary cirrhosis, viral-associated enteropathy, pericholangitis, chronic bronchitis, chronic sinusitis, asthma, uveitis, or graft versus host disease. 62. The method of aspect 61, wherein the disease or disorder is associated with an autoimmune disease is selected from Ulcerative colitis (UC), Crohn’s Disease (CD), psoriasis (PsO), or psoriatic arthritis (PsA). 63. Use of an antibody or antigen binding fragment thereof of any of aspects 1-31 or a composition of aspect 35 in the manufacture of a medicament for treatment of an IL-23R associated disease or disorder, particularly a disease or disorder associated with inflammatory, autoimmune inflammation diseases and/or related disorders. 64. The antibody or antigen binding fragment of any of aspects 1-31 or the composition of aspect 35 for use in the treatment of an IL-23R associated disease or disorder, particularly a disease or disorder associated with inflammatory, autoimmune inflammation diseases and/or related disorders [00477] A number of embodiments of the invention have been described. Nevertheless, it will be understood that various modifications may be made without departing from the spirit and scope of the invention. Accordingly, the following examples are intended to illustrate but not limit the scope of invention described in the claims. EXAMPLES [00478] The following is a description of various methods and materials used in the studies, and are put forth so as to provide those of ordinary skill in the art with a complete disclosure and description of how to make and use the present disclosure, and are not intended to limit the scope of what the inventors regard as their disclosure nor are they intended to represent that the experiments below were performed and are all of the experiments that may be performed. It is to be understood that exemplary descriptions written in the present tense were not necessarily performed, but rather that the descriptions can be performed to generate the data and the like associated with the teachings of the present disclosure. Efforts have been made to ensure accuracy with respect to numbers used (e.g., amounts, percentages, etc.), but some experimental errors and deviations should be accounted for. IL-23R antibody discovery and characterization summary [00479] Discovery of monoclonal antibodies (mAbs) that bind human interleukin (IL)-23 (IL- 23) receptor was done by both wild type mouse immunization and phage display and selection using proprietary Janssen de novo human and mouse Fab libraries. Recombinant human IL-23 receptor (IL- 23R) extracellular domain (ECD) protein (sequence shown in Table 3) was used as the antigen in both the immunization and phage display approaches, with the IL-23R ECD protein validated for IL-23 binding. A panel of human IL-23R binding mAbs was identified through both approaches that included both mouse antibodies from immunization and phage display and human antibodies from phage display only. Table 3. Amino acid sequence of human IL-23R ECD
[00480] All human IL-23R binding mAbs discovered were cloned with mouse IgG2a and mouse kappa constant domains and expressed recombinantly from mammalian cells for detailed characterization. Those mAbs originally identified as mouse antibodies were full mouse mAbs when recombinantly produced and those originally identified as human antibodies were human/mouse chimeric mAbs when recombinantly produced. The recombinant IL-23R binding mAbs expressed in mammalian cells were characterized as unpurified proteins in crude mammalian expression supernatants, as purified proteins or in both forms, with much of the characterization not requiring purified protein. Characterization of the IL-23R mAbs included determination of affinity to human and rat IL-23R ECD protein, determination of binding to recombinant cells lines expressing cell surface human IL-23R or primary human cells expressing IL-23R and determination of the number of human IL-23R ECD epitope/competition bins covered by the mAbs in this panel. [00481] The human IL-23R binding mAbs discovered, cloned, expressed, characterized and described here have a range of affinities to human IL-23R ECD. The antibodies demonstrate activities and binding capabilities which are unique to and/or better than other known IL-23R antibodies, including commercially available IL-23R antibodies. Most of the human IL-23R binding antibodies herein demonstrate and have higher affinity, some with substantially higher affinity, than the commercially available IL-23R mAbs tested. The antibodiesrecognize multiple distinct epitopes on the IL-23R extracellular domain. Some of the antibodies have cross-reactive binding to rat IL-23R ECD and bind to both human IL-23R and rat IL-23R, particularly binding to human IL-23R ECD and rat IL-23R ECD. Many of these mAbs show binding to both recombinant cell lines and primary human cells expressing human IL-23R, and demonstrate and have cell binding that is better than that of the commercially available IL-23R mAbs tested. The novel IL-23R antibodies provided herein comprise unique sequences and distinct and relevant binding characteristics and affinity, even among and between one another, as well as in comparison to other known and available antibodies including commercially available antibodies. Example 1: IL-23R mAb discovery [00482] Discovery of monoclonal antibodies (mAbs) that bind human interleukin (IL)-23 (IL- 23) receptor was done by both wild type mouse immunization and phage display. Immunization based IL-23R mAb discovery [00483] Recombinant human IL-23R extracellular (ECD) protein antigen was prepared with adjuvant for immunization. AJ and C3H mice were injected with prepared IL-23R antigen + CL413 IP on days 0, 14, 28, and 47. The surviving mice were euthanized on day 54, 7 days post final boost, and spleens and serum were harvested. Splenocytes from harvested spleens of 9 total individual mice, three A/J and six C3H, were stained with biotinylated human IL-23R/Fc and AF647 labeled ILT4/Fc (to exclude Fc binders). With gating set for IL-23R+ and ILT4/Fc-, a total of 7040 single B cells were sorted into 20-384 well plates containing single B cell (SBC) media. Six days post sort, supernatants were collected and B cells were lysed for all 20 plates of cultured single B cells. Supernatants were diluted 1:2 in PBS/BSA (0.4%) and stored at 4°C. Lysate plates were stored at -80°C. Supernatants were subsequently screened for binding to human IL-23R ECD protein and for IgG concentration using Meso Scale Discovery (MSD)-based assays. [00484] 876 SBC clones were identified with >10-fold IL-23R binding over background and the IgG quantification assay identified 451 clones with >2 ng/ml IgG, with 421 clones meeting both criteria. From these 421 clones, 384 were selected based on IL-23R binding over background being > 63-fold and IgG expression being >10 ng/ml. The antibody heavy chain (HC) and light chain (LC) variable regions (VH and VL, respectively) were cloned from the frozen lysates of the cultured single B cells using a 5’ RACE V-region cloning method. VH and VL regions obtained were cloned with mouse IgG 2a and mouse kappa constant regions, respectively, into separate mammalian cell expression vectors. Not all V-regions were successfully amplified and cloned. Plasmid DNA was prepared for all expression constructs generated for use in various scales of expression of the recombinant antibodies. Expression constructs were not sequenced and were considered non-clonal at this stage. Phage display based IL-23R mAb discovery [00485] Human IL-23 receptor binding Fabs were selected from in-house generated mouse de novo Fab-pIX phage display libraries or human de novo Fab-pIX display libraries as described in Shi et al., J Mol Biol 397:385-96, 2010 and Int. Pat. Publ. No. WO2009/085462; U.S. Pat. Publ. No. US2010/0021477, following standard protocols (Cheadle, E. J. et al. Antibody Engineering.907, 645– 666 (2012). [00486] Phage panning. In the phage selections, biotinylated purified recombinant biotinylated human IL-23 receptor (IL-23R) extracellular domain (ECD) was used as the antigen to capture and immobilize the phage binders. 42 panning experiments (I23RXP1 to 36, I23RXP53 to 57) using the mouse libraries and 8 panning experiments (I23RXP37 and 38, I23RXP47 to 52) using the human libraries were run. In each panning experiment, a specific combination of library(s) and panning conditions was used. Briefly, the phage libraries and paramagnetic streptavidin (SA) beads were blocked in 50% Chemiblocker (Millipore cat# 2170)/ 50% 1xTBST (Teknova cat# T0310) for one hour. Libraries were added to the SA beads to adsorb clones that bind non-specifically to the beads. SA beads were discarded and the pre-cleared library was added to biotinylated human IL-23R ECD. Binders were retrieved by addition of SA beads to form a bead/antigen/phage complex, which was washed in 1xTBST. After the final wash, phage was rescued by infection of log phase TG1 E. coli cells (OD600nm= 0.4-0.6). The phage-infected TG1 cells were spread on three 150 mm LB agar plates containing 75µg/ml carbenicillin and 1% glucose and grown overnight at 37°C. Phage was produced and subjected to additional panning. To increase selection pressure, the antigen concentration was reduced for each subsequent round: R1100nM, R250nM, R310nM, R410nM, R1-R4 all for 1 hour at room temperature; R55nM, overnight at 4ºC; R62.5nM, overnight at 4ºC. [00487] After multiple selection rounds, a polyclonal phage ELISA using human IL-23R ECD was performed to determine the enrichment of antigen-specific binders in individual panning experiments (representative polyclonal phage ELISA in FIG.1). [00488] Polyclonal phage ELISA. Briefly, 100µl of 20nM biotinylated human IL-23R ECD diluted in 1xTBS (Teknova cat# T9530) was captured on an NA-coated plate (Thermo cat# 15217). After an hour incubation at 37°C, the plate was washed 3 times in 300µl 1x TBST per well. 300µl of blocking buffer 50% Chemiblocker/50% 1xTBST was added to each well of the plate and incubated at room temperature for 1 hour. After blocking, the plate was washed 3 times with 300µl of 1xTBST per well. Polyclonal phage output for each panning round of each panning experiment was diluted 1/100 diluted in assay buffer (10% Chemiblocker /90% 1xTBST). 100µL of these diluted phage outputs was added to the blocked ELISA plate and incubated at room temperature for 1 hour to allow the binding of Fab displayed on the phage particles to the immobilized human IL-23R ECD. Following the incubation, the plate was washed 3 times with 1xTBST. 100µl of HRP-conjugated anti-M13 (pVIII) antibody (GE Healthcare cat# 27942101) diluted 1:2500 in assay buffer was added to the plate and incubated at room temperature. After 1 hour incubation, the plate was washed 6 times with 300µl of 1xTBST per well. 100µL of prepared BM chemiluminescence ELISA substrate (Roche cat# 11582950001) was added to the plate. The chemiluminescence or relative light unit (RLU) was measured in an Envision plate reader. [00489] Phage collected from panning experiments which demonstrated enrichment for human IL-23R ECD binders, were used to express monoclonal Fab proteins in E. coli for primary screening. [00490] Fab production. Briefly, plasmid DNA was isolated and purified from glycerol stocks of specific rounds of phage panning experiments that were identified as demonstrating enrichment of binders to human IL-23 receptor and transformed into TG-1 E. coli cells and grown on LB agar plates overnight. The plates of transformants were used for (i) colony PCR and sequencing of the V-regions and (ii) starter cultures for Fab production. For Fab production, the overnight cultures were diluted 10-100 fold in new media, grown for 5-6 hours at 37°C and Fab production induced by the addition of fresh media containing IPTG. Induced cultures were grown overnight at 30°C. The cultures were spun down and the bacterial pellet was lysed using BugBuster™ (Millipore) to release the soluble Fab proteins. The cell lysates were cleared by centrifugation and the supernatants were used for Fab ELISA. [00491] Monoclonal Fab lysates that were prepared from the enriched Fab libraries were screened by ELISA for binding to human IL-23 receptor and lack of binding to a negative control antigen, mouse IL-6. [00492] Monoclonal Fab screening. Black maxisorp plates (ThermoFisher Scientific, Cat#437111) were coated with 100µl of 10ng/µl goat anti-mouse Fab2 (Jackson Immuno Research, Code#115-005-072) or 4 ng/µl of sheep anti-human Fd (The Binding Site Group, Product Code AU075). After overnight incubation at 4ºC, the coated plates were blocked with 250µl of Chemiblocker (Milipore, Cat# 2170) and incubated at room temperature for 1 hour. 100µl of each Fab sample were added to wells and the plates were incubated at room temperature for 1 hour with shaking at 20rpm, followed by 5 washes with 1X TBST. 100 µl of 20nM biotinylated human IL-23 receptor ECD or murine IL-6 (counter screening) were added to wells and incubated at room temperature for 1 hour with shaking 20rpm, followed by 5 washes with 1X TBST. 100µl of 1:5000 strepavidin HRP were added, and the plates incubated at room temperature for 40 minutes, followed by 3 washes with 1X TBST. 100µL per well of prepared BM chemiluminescence ELISA substrate (Roche cat# 11582950001) was added to the plate. The chemiluminescence or relative light unit (RLU) was measured in an Envision plate reader. [00493] Fab clones meeting the selection criteria of binding to human IL-23 receptor and not binding to a negative control antigen, mouse IL-6, were sequenced to identify the unique Fabs (representative monoclonal Fab ELISA in FIG.2). [00494] Heavy chain (HC) and light chain (LC) variable (V) regions (VH and VL, respectively) of the unique Fab were cloned into mammalian expression vectors to express recombinant mAbs with murine IgG2a / murine Kappa constant regions. Plasmid DNA was prepared for all expression constructs generated for use in various scales of expression of the recombinant antibodies. [00495] Cloning VH and VL of IL-23R binding Fab hits. Two pcDNA3.1 derived mammalian expression vectors (vDR000368 and vDR000961) were used to generate the single gene constructs encoding a heavy chain (HC) or light chain (LC) for each Fab hit. Each vector contains a human cytomegalovirus (hCMV) promoter to drive the expression of the HC and LC and both contain the ampicillin resistance gene (Amp(R)) to facilitate cloning. vDR000368 has unique HindIII and DraIII restriction enzyme sites for VH cloning and also a mouse IgG2a constant region; vDR000961 has unique HindIII and Tth111I restriction enzyme sites for VL cloning and also a mouse Kappa constant region. IL-23R mAb expression and purification [00496] Recombinant IL-23R binding mAbs discovered from both the immunization and phage display strategies were transiently expressed in either ExpiCHO or HEK Expi293™ cells in various expression volumes from 2 ml to 500 ml using prepared and quantitated plasmid DNA of the heavy chain (HC) and light chain (LC) mammalian expression constructs generated for these mAbs. [00497] Expression in transiently transfected HEK Expi293™ cells. HEK Expi293™ cells (Thermo cat # A14527) were grown in Expi293™ expression media (Thermo cat # A1435101) at 37°C shaking at 125RPM with 8% CO 2 . The cells were transfected at 2.5 x 10 6 cells per ml using Expi293™ Expression Kit (Thermo cat# A14524). For each liter of cells transfected, 1mg of total DNA was diluted in 25ml of Opti-MEM (Thermo cat # 319850620) and 2.6ml of Expi293™ reagent was diluted in 25ml of Opti-MEM and incubated for 5 minutes at room temperature. The diluted DNA and diluted Expi293 reagent were combined and incubated for 20 minutes at room temperature. The DNA complex was then added to the cells and the cells placed in the shaking incubator overnight. The next day after transfection, 5ml of Enhancer 1 was diluted into 50ml of Enhancer 2 and the total volume of the two Enhancers was added to the cells. The transfected cells were placed back into the incubator for 4 days until harvested. The cells were removed by centrifugation at 4,500g for 35 minutes then the cleared culture is filtered with a 0.2µm filter prior to checking expression levels. This protocol can be used with varying expression volumes by adjusting reagents in a linear manner. When transfection is done with 96-well plates incubation is done in an incubator with a 3 mm shaking diameter set at 1,000 RPM. Expression was quantitated by Octet using Protein A biosensors. Murine IgG2 (Sigma Cat #M9144) was used as the standard. The samples and the standard were diluted with spent Expi293 media. The standard curve was generated with two-fold dilutions starting at 100µg/ml, using the linear portion. The samples were diluted 1:10 for measurement. The calculations were performed by the Forte Biosystems software. [00498] Expression in transiently transfected ExpiCHO cells. Transient transfection using ExpiCHO-S™ cells (ThermoFisher Scientific, Cat # A29127) with purified DNA plasmid following manufacturer’s recommendations. Briefly, ExpiCHO-S™ cells were maintained in suspension in ExpiCHO™ expression medium (ThermoFisher Scientific, Cat # A29100) in a shaking incubator set at 37 ° C, 8% CO2 and 125 RPM. The cells were passaged so that on the day of transfection, dilution down to 6.0 x 10 6 cells per ml could be achieved, maintaining cell viability at 98% or better. Transient transfections were done using the ExpiFectamine™ CHO transfection kit (ThermoFisher Scientific Cat # A29131). For each ml of diluted cells to be transfected, one microgram of plasmid DNA is used and diluted into OptiPRO™ SFM complexation medium. ExpiFectamine™ CHO reagent is used at a 1:3 ratio (v/v, DNA:reagent) and also diluted into OptiPRO™. The diluted DNA and transfection reagent were combined for one minute, allowing DNA/lipid complex formation, and then added to the cells. After overnight incubation, ExpiCHO™ feed and ExpiFectamine™ CHO enhancer were added to the cells. Cells were cultured with shaking at 32 ° C for five days prior to harvesting the culture supernatants. Culture supernatants from the transiently transfected ExpiCHO- S™ cells were harvested by clarifying through centrifugation (35 min, 6,500 rpm) followed by filtration (0.2µ PES membrane, Corning). [00499] The crude mammalian expression supernatants, after quantitation of mAb concentration, were used directly for some characterization of the unpurified mAbs contained within. Some IL-23R mAbs were purified using a routine Protein A purification protocol and characterized as purified mAbs. [00500] Protein A purification of mAbs expressed in transient transfections. Pilot scale (0.3- 3 mgs) purifications were performed on the AKTA Xpress chromatography system and large-scale (3 mgs or greater) purifications were performed using the AKTA FPLC chromatography systems. The purification procedures for pilot and large-scale preps were identical. Briefly, harvested, clarified and filtered supernatants from transiently transfected mammalian cells were loaded onto an equilibrated (PBS, pH 7.2) HiTrap MabSelect Sure Protein A column (GE Healthcare) at a relative concentration of ~30 mg protein per ml of resin. After loading, the column was washed with PBS, pH7.2 and protein eluted with 10 column volumes of 0.1 M Na-Acetate, pH 3.5. The protein fractions were neutralized immediately by elution into tubes containing 2.0 M Tris, pH 7 at 20% the elution fraction volume. Peak fractions were pooled, further neutralized, if necessary, filtered (0.2 µm) and dialyzed against 3 changes of PBS, pH 7.2 overnight at 4°C. The next day, samples were removed from dialysis, filtered (0.2 µm) and the protein concentration determined by absorbance at 280nm. The quality of the purified proteins was assessed by SDS-PAGE and analytical size exclusion HPLC (Dionex HPLC system). Endotoxin levels were measured using a LAL assay (Pyrotell®-T, Associates of Cape Cod). Purified proteins were stored at 4°C. Exemplary IL-23R mAbs [00501] Examples of immunization based IL-23R antibodies or antigen binding fragments of the present disclosure are summarized in Table 4, Table 5 and Table 6: Table 4. HC and LC AA Sequences of Exemplary Immunization Based IL-23R Antibodies
Table 5. VH and VL AA Sequences of Exemplary Immunization Based IL-23R Antibodies Table 6. CDR AA Sequences of Exemplary Immunization Based IL-23R Antibodies
[00502] Examples of phage display based IL-23R antibodies or antigen binding fragments of the present disclosure are summarized in Table 7, Table 8, and Table 9. All of the phage display based antibodies with the exception of I23RB332 and I23RB7 were derived from the human phage display and are human antibodies. Antibody I23RB332, corresponding to VH SEQ ID NO:898 and VL SEQ ID NO:899 and also antibody I23RB7, corresponding to VH SEQ ID NO:798 and VL SEQ ID NO:799, are mouse antibodies. Table 7. HC and LC AA Sequences of Exemplary Phage Display Based IL-23R antibodies
Table 8. VH and VL AA Sequences of Examplary Phage Display Based IL-23R antibodies
Table 9. CDR AA Sequences of Exemplary Phage Display Based IL-23R antibodies
Example 2: Binding kinetics and affinity measurements [00503] Affinity of the IL-23R mAbs for human and rat IL-23R ECD protein was determined using both purified and unpurified mAbs by Surface Plasmon Resonance (SPR) and Biolayer Interferometry (BLI) methods. BLI was also used to determine how many different epitopes on human IL-23R ECD are bound by the panel of immunization and phage display derived IL-23R mAbs through competition binding experiments. Commercially available IL-23R mAbs were included in the binding studies to IL-23R protein for comparison. The commercial antibodies evaluated were: Anti-IL23R, Rab Mab, clone EPR22838-4, AbCam cat #222104; Anti-IL23R, Mouse IgG2b, clone #218213, R&D cat #MAB14001; Anti-IL23R, Mouse IgG1, clone #15N6C6, ThermoFisher cat #MA5-24804; Anti-IL23R, Mouse IgG1, clone #ABM25G4, Abcam cat #ABM25G4; Anti-IL23R, Mouse IgG2b, LSBio cat #LS-C37068; Anti-IL23R, Mouse IgG2a, LSBio cat #LS-C308468; and Anti-IL23R, Mouse IgG1, clone #5H9, LSBio cat #LS-C340289. Affinity measurements [00504] Surface Plasmon Resonance (SPR) and Biolayer Interferometry are label-free detection methods used to investigate biomolecular interactions. By monitoring small changes in mass on a sensor surface, these direct real-time binding assays provide qualitative and quantitative data about the interaction between biomolecules; i.e. determination of equilibrium binding constant (affinity, KD) and kinetic rate constants (ka/kd; rate of complex association ka, and rate of complex dissociation kd). This method is useful in studies of protein-protein and protein-nucleic acid interactions, as well as interactions between proteins and small molecules. Here, interactions between IL-23R antibodies and human IL-23R and rat IL-23R extracellular domain (ECD) proteins were investigated. [00505] The human IL-23R ECD sequence (SEQ ID NO:1) is provided above in Table 3. Sequence comparison and alignment of the human and rat IL-23R extracellular domain sequences demonstrates 76.74% sequence identity. The rat IL-23R ECD sequence (F1LX96 amino acids 24-354) is provided below: GIATINCSGNMWVEPGEIFQMGMNVSVYCQEALKNCRPRNLHFYKNGFKERFHITRINRT TA RVWYKGFSEPHASMYCTAECPGRFQETLICGKDISSGYPPDAPSNMTCVIYEYSGNMTCT WN TGKPTYIDTKYTVHVKSLETEEQQQYLASNYVNISTDSLQGGRKYLVWVQAVNALGMENS Q QLQVHLDDIVIPSPSIISRAETTNANVPKTIIYWKSKIMTGKVFCEMRYKATTNQTWNVK EFD TNYTYVQQSEFYLEPNSKYVFQVRCQGTGKRNWQPWSSPFVHQTPQTASQVTSKPPHEPQ KI EMLTATIFKGHSTSDNSQDIG (SEQ ID NO:1267) [00506] Affinity by SPR using ProteOn. Affinity measurements using Surface Plasmon Resonance (SPR) were performed using a ProteOn XPR36 system (BioRad). A biosensor surface was prepared by coupling anti-Mouse IgG Fc (Jackson cat# 315-005-046) to the modified alginate polymer layer surface of a GLC chip (BioRad, Cat#176-5011) using the manufacturer instructions for amine-coupling chemistry. Approximately 6000 RU (response units) of mAbs were immobilized. The kinetic experiments were performed at 25ºC in running buffer (DPBS+0.01%P20+100µg/ml BSA). To perform kinetic experiments, approximately 250 RU of mAbs were captured followed by injections of human IL-23R at concentrations ranging from 1.56nM to 400nM (in a 4-fold serial dilution). The association phase was monitored for 3 minutes at 50 µL/min, then followed by 10 minutes of buffer flow (dissociation phase). The chip surface was regenerated with two 18 second pulses of 100 mM H3PO4 (Sigma, Cat#7961) at 100 µL/min. The collected data were processed using ProteOn Manager software. First, the data was corrected for background using inter-spots. Then, double reference subtraction of the data was performed by using the buffer injection for analyte injections. The kinetic analysis of the data was performed using a Langmuir 1:1 binding model. The result for each mAb was reported in the format of Ka (On-rate), Kd (Off-rate) and KD (equilibrium dissociation constant). [00507] Affinity by SPR using Biacore 8K. Affinity measurements using Surface Plasmon Resonance (SPR) were performed using a Biacore 8K system (Cytiva). A biosensor surface was prepared by coupling anti-Mouse IgG Fc (Jackson cat# 315-005-046) to the surface of a CM5 chip using the manufacturer instructions for amine-coupling chemistry. Approximately 9000-10000 RU (response units) of mAbs were immobilized. The kinetic experiments were performed at 25ºC in running buffer 1X of (HBS-P+ Buffer 10× (Cytiva# BR100671) + 100µg/ml BSA). To perform kinetic experiments, approximately 150 RU of mAbs were captured followed by injections of human IL-23R or rat IL-23R at concentrations ranging from 0.8nM to 500nM (in a 5-fold serial dilution). The association phase was monitored for 3 minutes at 50 µL/min, then followed by 30 minutes of buffer flow (dissociation phase). The chip surface was regenerated with four 20 second pulses of 0.85% H3PO4 (Sigma, Cat#7961) at 100 µL/min. The collected data were processed using Biacore insight Evaluation software (Version 3.0.12.15655). The kinetic analysis of the data was performed using a Langmuir 1:1 binding model. The result for each mAb was reported in the format of Ka (On- rate), Kd (Off-rate) and KD (equilibrium dissociation constant). [00508] Affinity by BLI using Octet Red 384. Affinity measurements using Biolayer Interferometry (BLI) were performed using an Octet Red 384 system (Sartorius). Antibodies were loaded on to Protein A biosensors (Sartorius, Cat#18-5010) to approximately a 1 nm shift. The kinetic experiments were performed at 25ºC in running buffer of (DPBS + 0.02% P20 + 1mg/ml BSA). To perform kinetic experiments, both human and rat IL-23R are associated at concentrations ranging from 1.37nM to 1000nM (in a 3-fold serial dilution). The association phase was monitored for 3 minutes with shaking at 1000rpm, followed dissociation in buffer for 5 minutes, with shaking at 1000rpm. The collected data was processed using Octet Evaluation software (Version 10). The kinetic analysis of the data was performed using a Langmuir 1:1 binding model. The result for each mAb was reported in the format of Ka (On-rate), Kd (Off-rate) and KD (equilibrium dissociation constant). [00509] Six of the seven commercially available mAbs tested for binding kinetics by SPR or BLI were mouse IgG mAbs that had weak signal above background or no binding at the highest 4uM concentration of human IL-23R extracellular domain protein (ECD) tested. The commercially available Abcam rabbit monoclonal antibody (RabMab) (catalog# 222104) showed slightly stronger binding to human IL-23R ECD compared with the other 6 commercially available mAbs, but had a KD value >100nM. The mAbs derived from phage panning and human IL-23R immunizations have a range of affinities from <51pM to >263nM and all have better human IL-23R ECD binding affinity than the commercially available R&D Systems human IL-23R mAb, MAB14001. MAB14001 showed no binding to human IL-23R ECD in SPR but had measurable binding to human IL-23R expressing cells in flow cytometry experiments. Most of the phage display and immunization derived mAbs also have better human IL-23R ECD binding affinity than the Abcam mAb (catalog# 222104). Only some of the human IL-23R mAbs showed binding to rat IL-23R ECD. Affinities determined for the commercially available human IL-23R binding mAbs and those derived from phage panning and human IL-23R immunizations are summarized in Table 10. [00510] Antibodies I23RB5, I23RB101, I23RB6, I23RB8, I23RB9, I23RB10, and I23RB80 show no binding or undetectable or very weak binding in the assays provided in Table 10. Other antibodies that showed no binding or undetectable or very weak binding are I23RB104, I23RB149, I23RB189, I23RB273, I23RB278, I23RB328, I23RB329, I23RB330 and I23RB332. These antibodies are useful in experiments and assays including as negative control antibodies, providing ‘true’ negatives isolated procedurally with the IL23R binders herein. For instance, I23RB5 has been used as a negative comtrol in various experiments and assays, including as provided herein. Table 10. IL-23R mAb affinities for human and rat IL-23R ECD
Note: *If koff is slower than the dissociation limit imposed by the data collection time, koff reported as < the koff limit (Koff is <2.89E-05) *Binding not detectable = No measureable binding signal up to the highest concentration of antigen tested *Weak binding = weak binding signal above background at the highest concentration of antigen tested IL-23R mAb epitope binning [00511] Recombinant mAbs derived from human IL-23R phage panning and immunizations were paired together and evaluated for competitive binding to the human IL-23R ECD using Biolayer Interferometry (BLI) performed on the Sartorius Octet Red 384 instrument to group them into epitope bins, where mAbs that competed were grouped within the same bin or overlapping bins. If any mAbs did not demonstrate competition when paired with the other mAbs they were classified in their own unique bin. Sufficient binding affinity and/or concentration were required to interpret competitive binding results, and mAbs with affinities and/or concentrations that were too low were not included in an epitope bin with the bin being deemed inconclusive.4 purified antibodies from the phage panning and 11 purified antibodies from the immunization campaign that exhibited the strongest binding to IL- 23R protein, were paired against themselves in a full matrix. The remaining mAbs derived from immunizations or phage display were evaluated as unpurified mAb proteins in supernatants and were only binned against the purified mAb from each bin with the highest affinity. [00512] Epitope Binning by BLI using Octet Red 384. Epitope Binning using Biolayer Interferometry (BLI) was performed using an Octet Red 384 system (Sartorius). To perform epitope binning, experiments were performed at 25ºC in running buffer of (DPBS + 0.02% P20 + 1mg/ml BSA). Biotinylated human IL-23R was loaded on to Streptavidin biosensors (Sartorius, Cat#18-5019) to approximately a 1 nm shift. Antibodies were diluted to 333nM where concentration allowed. Antibody 1 was associated for 2 minutes. Excess was washed off with a 20 seconds dip into assay buffer. Antibody 2 was associated for 2 minutes. The collected data was processed using epitope binning module with the Octet Evaluation software (Version 10). [00513] Thirty-seven of the anti-IL-23R mAbs derived from phage panning and immunizations were evaluated in epitope binning experiments resulting in at least nine unique bins covering 32 out of the 37 mAbs tested. Three of the remaining five mAbs fell within a unique bin and these mAbs have not been paired with each other, so it is not known if they share the same epitope bin or if there are additional bins within this set. The epitope bins and the mAbs included in each are summarized in Table 11. The diverse set of IL-23R binding sites reflected in these 9(+) epitope bins indicates that, in contrast to the single binding site of MAB14001, the panel of IL-23R mAbs offers a range IL-23R mAb:IL-23R interactions, which may improve receptor binding/detection, either through multiplexing (using a cocktail of multiple IL-23R mAbs functioning in a non-competitive fashion to boost signal) or by targeting a particular epitope that is more accessible to mAb binding. Table 11. Epitope binning of human IL-23R binding mAbs on human IL-23R
[00514] As shown in Table 11, anti-IL-23R mAbs (unpurified in supernatant and purified*) have been grouped into 9 bins using BLI (Octet RED384). mAbs in Bins 6, 7, 8 & 9 are defined as showing competition with at least one mAb in a previously identified Bin(s) shown in parentheses. I23RB74, I23RB77 and I23RB102 are listed as unique based on not competing with the purified antibodies they were tested against. These antibodies have not been tested against each other so they may or may not be in separate bins. mAbs listed as indeterminant are samples that may either be too low in concentration or too weak in affinity for a conclusive result. Binding to human IL-23R transfected cell lines [00515] Recombinant human IL-23R binding mAbs derived from phage panning and immunizations were tested for binding to cell surface human IL-23R expressed on stably transfected iLite and/or HEK cell lines using flow cytometry. The mAbs were tested as either purified proteins or unpurified proteins in crude mammalian cell expression supernatants using either a single or multiple mAb concentrations. Whether the IL-23R mAbs can bind primary human cells expressing IL-23R was also determined by flow cytometry but with purified mAbs only. Commercially available IL-23R mAbs were included in the binding studies to IL-23R expressing cells for comparison. [00516] Human IL-23R iLiTe cell single concentration mAb Binding. Anti-IL-23R mouse IgG2a mAbs derived from phage panning were tested for binding to human IL-23R expressing iLiTe cells, where a PE conjugated anti mouse secondary antibody detected mAbs bound to the receptor on the cells. Human IL-23R expressing iLite® IL-23 Assay Ready Cells (Eurodiagnostica, Catalog# BM4023) were thawed from cryopreservation, placed in 25 mL RPMI-1640 plus GlutaMAX-1 (ThermoFisher Scientific, Catalog# 72400-047) containing 10% FBS (Gibco Life-Technologies, Catalog# 16140-063) and 1% Penicillin-Streptomycin (Gibco Life-Technologies, Catalog# 15140- 122), and incubated overnight at 37°C, 5% CO 2 . The next day 100,000 cells were added to each well of a 96 well V bottom plate (Costar, Catalog# 3357), centrifuged at 450x gravity for 2 minutes, and then supernatants were decanted. Cells were then resuspended in 100 µL/well of 10% human serum (Valley Biomedical, Catalog# HP1022) in 1xDPBS (Gibco Life-Technologies, Catalog# 14190-136) and incubated for 30 minutes on ice followed by centrifugation and decanting of the supernatants. Antibodies diluted to 3 µg/mL in Stain Buffer (BSA) (BD Pharmagen, Catalog# 554657) were added at 100 µL/well and incubated on ice for 50 minutes, then plates were centrifuged and supernatants were decanted. Goat anti-mouse PE conjugated secondary antibody (Jackson ImmunoResearch Catalog# 115-116-146) diluted 1:200 in Stain Buffer was added at 100 µL/well and incubated on ice for 30 minutes followed by centrifugation and decanting of the supernatants. Cells were washed by adding 100 µL/well of Stain Buffer followed by centrifugation and decanting of the supernatants. Cells were resuspended in 100 µL/well of Stain Buffer and analyzed on the Becton Dickenson LSR II FACS instrument with HTS module. Data was analyzed using FlowJo software (Treestar) to obtain geometric mean fluorescence intensities. [00517] Human IL-23R iLiTe cell concentration response mAb binding. Anti-IL-23R mouse IgG2a mAbs derived from phage panning were tested for concentration dependent binding to human IL-23R expressing iLiTe cells relative to a mouse IgG2a isotype negative control mAb and the commercially available MAB14001 positive control mAb from R&D Systems, where a PE conjugated anti mouse secondary antibody detected mAbs bound to the receptor on the cells. Human IL-23R expressing iLite® IL-23 Assay Ready Cells (Eurodiagnostica, Catalog# BM4023) were thawed from cryopreservation, placed in 25 mL RPMI-1640 plus GlutaMAX-1 (ThermoFisher Scientific, Catalog# 72400-047) containing 10% FBS (Gibco Life-Technologies, Catalog# 16140-063) and 1% Penicillin- Streptomycin (Gibco Life-Technologies, Catalog# 15140-122), and incubated overnight at 37°C, 5% CO2. The next day 100,000 cells were added to each well of a 96 well V bottom plate (Costar, Catalog# 3357), centrifuged at 450x gravity for 2 minutes, and then supernatants were decanted. Antibodies were diluted in Stain Buffer (BSA) (BD Pharmagen, Catalog# 554657) and added at 50 µL/well, and mixed. Plates were incubated on ice for 50 minutes, then plates were centrifuged and supernatants were decanted. Goat anti-mouse PE conjugated secondary antibody (Jackson ImmunoResearch Catalog# 115-116-146) diluted 1:200 in Stain Buffer was added at 100 µL/well and incubated on ice for 30 minutes followed by centrifugation and decanting of the supernatants. Cells were washed by adding 200 µL/well of Stain Buffer followed by centrifugation and decanting of the supernatants. Cells were resuspended in 100 µL/well of Stain Buffer, transferred in quadruplicate to a 384 well plate (Greiner, Catalog# 781281) and analyzed on the Becton Dickenson LSR II FACS instrument with HTS module. Data was analyzed using FlowJo software (Treestar) to obtain geometric mean fluorescence intensities, and geometric mean fluorescence intensities were plotted over log mAb concentrations fitted with a sigmoidal dose response curve with variable slope using GraphPad Prism. [00518] Five out of an initial 10 phage derived anti-IL-23R mAbs had measurable binding signals on human IL-23R iLite cells in a single concentration flow cytometry experiment using purified mAb proteins, which include I23RB1, I23RB2, I23RB3, I23RB4, I23RB7 (Table 12, Expt A & B). Subsequent concentration response binding experiments showed all five of these mAbs bound to human IL-23R iLite cells better than the R&D Systems MAB14001 mAb, with binding ranked in the following order I23RB1=I23RB4>I23RB7>I23RB3>I23RB2>MAB14001 (Table 12, Expt C). The lack of binding by I23RB5 repeated, giving the same signal as the mouse IgG 2a isotype control. [00519] 83 additional human IL-23R binding mAbs from phage panning and immunizations were also tested for binding to human IL-23R expressing HEK cells as either purified proteins or unpurified proteins in crude expression supernatants from transiently transfected CHO cells. [00520] HEK-IL-23R cell concentration response mAb binding (8-point, 96-well assay). The immunization- and phage-derived anti-IL-23R mouse IgG2a mAbs were tested for concentration dependent binding to human IL-23R expressing HEK-IL-23R cells relative to a mouse IgG2a negative control mAb that does not bind to IL-23R on cells, I23RB5, where a 647 conjugated anti mouse secondary antibody detected antibody bound to the receptor on the cells. HEK-IL-23R and HEK- parental (pre-labeled with CellTrackerBlue, ThermoFisher, Cat# C2110) cells were washed with dPBS (Gibco, Cat# 14190-136), detached with Accutase (StemCell Technologies, Cat# 7920), resuspended in Assay medium (RPMI-1640 (ThermoFisher, Cat# 11875135) with 10% fetal bovine serum (Gibco, Cat# A31604-01)), pelleted by centrifugation (3 min, 600 g), and resuspended at 4800 cells/µL. HEK-IL-23R and HEK-parental cells (12.5 µL of each, 120000 cells total) were plated in 2X replicate on 96-well V-bottom plates (Corning, Cat# 3357) into 37°C warmed Assay medium containing serially diluted IL-23R mAbs to a final volume of 150 µL. IL-23R mAbs were allowed to bind to cells for 30 minutes, at 37°C. Cells were next washed twice in ice-cold stain buffer (BD Biosciences, Cat# 554657), then exposed to the anti-mouse-647 detection antibody (Jackson ImmunoResearch, Cat# 115-606-062) diluted 1:350 in ice-cold stain buffer for 30 minutes on ice. Cells were next washed twice in ice-cold stain buffer, then resuspended in a final volume of 30 µL with Sytox Green viability dye (ThermoFisher, Cat # S7020). Plates were kept on ice until run for analysis on the iQue. All washes were performed by centrifugation (800 rcf, 3 minutes) followed by flick decantation to remove supernatants. Cell-binding to HEK-IL-23R cells was measured with FlowJo, by gating for single, viable cells and determining the geometric mean fluorescence intensity (MFI) for the 647 detection antibody. Geometric mean fluorescence intensities were plotted over log mAb concentrations fitted with a dose response curve with variable slope using GraphPad Prism. Cell binders were scored as those mAbs with MFI signals [S] at the maximum used concentration that were greater than baseline MFI signal [B] + 3*StDev, where [B] is the MFI signal detected with the negative control, I23RB5, at an equivalent concentration. [00521] HEK-IL-23R cell concentration response mAb binding (11-point, 384-well assay). The immunization- and phage-derived anti-IL-23R mouse IgG 2a mAbs were tested for concentration dependent binding to human IL-23R expressing HEK-IL-23R cells relative to a mouse IgG 2a negative control mAb that does not bind to IL-23R on cells, I23RB5, where a 647 conjugated anti mouse secondary antibody detected antibody bound to the receptor on the cells. HEK-IL-23R and HEK- parental (pre-labeled with CellTrackerBlue, ThermoFisher, Cat# C2110) cells were washed with dPBS (Gibco, Cat# 14190-136), detached with Accutase (StemCell Technologies, Cat# 7920), resuspended in Assay medium (RPMI-1640 (ThermoFisher, Cat# 11875135) with 10% fetal bovine serum (Gibco, Cat# A31604-01), pelleted by centrifugation (3 min, 600 g), and resuspended at 2500 cells/uL. HEK-IL-23R and HEK-parental cells (10 µL of each, 50000 cells total) were plated in 4X replicate on 384-well V-bottom plates (Greiner, Cat# 781281) into 37°C warmed Assay medium containing serially diluted IL-23R mAbs, respectively, to a final volume of 80 µL. IL-23R mAbs were allowed to bind to cells for 30 minutes, at 37°C. Cells were next washed once in ice-cold stain buffer (BD Biosciences, Cat# 554657), then exposed to the anti-mouse-647 detection antibody (Jackson ImmunoResearch, Cat# 115-606-062) diluted 1:350 in ice-cold stain buffer for 30 minutes on ice. Cells were next washed twice in ice-cold stain buffer, then resuspended in a final volume of 10 µL with Sytox Green viability dye (ThermoFisher, Cat # S7020). Plates were kept on ice until run for analysis on the iQue. All washes were performed by centrifugation (800 rcf, 3 minutes) followed by automated aspiration to remove supernatants with plate washers. Cell-binding to HEK-IL-23R cells was measured with FlowJo, by gating for single, viable cells and determining the geometric mean fluorescence intensity (MFI) for the 647 detection antibody. Geometric mean fluorescence intensities were plotted over log mAb concentrations fitted with a dose response curve with variable slope using GraphPad Prism. Cell binders were scored as those mAbs with MFI signals [S] at the maximum used concentration that were greater than baseline MFI signal [B] + 3*StDev, where [B] is the MFI signal detected with the negative control, I23RB5, at an equivalent concentration. [00467] 11 of the 83 additional human IL-23R binding mAbs did not bind cells at thresholds above background (MFI > background * 3X Stdev). Of the 72 IL-23R mAbs that did exhibit cell binding to IL-23R above background, EC50 values ranged from 0.1nM to >50nM (Table 12, Expt D & E). Of these cell binders, 34 mAbs presented with MFI (@ 6.4 nM) values (Table 12, Expt E) that exceeded I23RB3, which together with I23RB2, both showed superior binding compared to MAB14001 [Table 12, Expts A-C (higher MFI, lower EC50)], indicating that these 34 mAbs are also superior to MAB14001 for the detection of IL-23R on cells. These 34 mAbs include I23RB1, I23RB102, I23RB148, I23RB155, I23RB156, I23RB157, I23RB160, I23RB162, I23RB166, I23RB27, I23RB270, I23RB30, I23RB318, I23RB32, I23RB33, I23RB36, I23RB39, I23RB4, I23RB42, I23RB45, I23RB47, I23RB58, I23RB65, I23RB7, I23RB73, I23RB74, I23RB76, I23RB77, I23RB81, I23RB82, I23RB86, I23RB92, I23RB93, and I23RB94. Human IL-23R binding mAbs I23RB71, I23RB165, and I23RB173 had EC50 values < 9.7nM (Table 12, Expt E), placing them in the >72 percentile (rank of mAbs Experiment E EC50), and demonstrating they are also superior to MAB14001 for the detection of IL-23R on cells. [00468] The results of IL-23R binding mAbs affinities to human IL-23R expressed on stably transfected iLite and HEK cell lines are shown in Table 12. Table 12. Binding of IL-23R mAbs to human IL-23R expressing cell lines
[00469] mAbs ranking is shown in Table 12. For Experiment D, the 77 mAbs tested were ranked in ascending order by EC50. The relative position of all mAbs is indicated by the %, with the top performers (lowest EC50’s) showing the highest %'s. A percentage range is included for mAbs that could not be accurately quantified due to poor cell binding or EC50's > 50. For Experiment E (MFI), the 61 mAbs tested were ranked in descending order by MFI at 6.4 nM. The relative position of the mAbs is indicated by the %, with the top performers (highest MFI’s) showing the highest %'s. 26 mAbs that were not tested because of poor cell binding in Experiment D were included in the rankings and pre-ranked at the bottom (range <31%). For experiment E (EC50), the 56 mAbs tested were ranked in ascending order by EC50 values. The relative position of the mAbs is indicated by the %, with the top performers (lowest EC50’s) showing the highest %'s.26 mAbs that were not tested because of poor cell binding in Experiment D were included in the rankings and pre-ranked at the bottom (range <32%). A percentage range is included for mAbs that could not be accurately quantified due to EC50's > 50. Example 3: IL-23R mAbs detect IL-23R on the surface of primary human immune cells [00470] Primary cell culture. Cryopreserved peripheral blood mononuclear cells (PBMCs) from healthy donors (AllCells) were thawed and washed twice in ImmunoCult-XF T cell expansion medium (XF-TCEM) (StemCell Technologies cat# 10981) supplemented with CTL anti-aggregate wash (Cellular Technology Limited cat# CTL-AA-001). The cells were counted, resuspended at 2- 6x10 5 cells per mL XF-TCEM supplemented with penicillin and streptomycin (Sigma-Aldrich cat# P0781-100ML) and 100 ng/mL IL-1β (Biolegend cat# 579404), and cultured in flasks coated with 10 µg/mL anti-CD3 (clone UCHT1) (BD Pharmingen cat# 555329) for 4 days at 37°C in 5% CO 2 . On day 4 of culture, PBMCs were collected, washed twice in RPMI-1640 supplemented with 0.1% BSA (RPMI-BSA), and counted. Cells were stained directly with anti-IL-23R mAbs or incubated in RPMI- BSA in upright tissue culture flasks for >4 hours at 37°C in 5% CO 2 prior to staining. When functional IL-23R expression (i.e., IL-23 responsiveness) was assessed, cells were incubated in RPMI-BSA in upright tissue culture flasks for >4 hours at 37°C in 5% CO 2 . [00471] Measurement of IL-23-induced STAT3 phosphorylation. To assess IL-23 responsiveness, a total of 6x10 4 ‘cytokine-starved’ cells in 30 µL RPMI-BSA was transferred into each well of a 384-well plate. The cells were stimulated with a serial titration of IL-23 (internally sourced from Janssen). After a 30-minute incubation at 37°C in 5% CO 2 , the cells were transferred onto ice for 10 minutes and then lysed. Cell lysates were stored at -80°C. After thawing at room temperature, 25 µL of each lysate were transferred to MSD plates treated with ‘Blocker A’ provided with the MSD phospho-STAT panel kit (Meso Scale Discovery cat# K15202D). Following a one- hour incubation with shaking, the plates were washed with Tris wash buffer. A total of 25 µL detection antibodies was added to each well, and the plates were incubated for an additional hour with shaking. The plates were then washed three times. After the final wash, 150 µL read buffer were added to each well before reading the plates on a Meso Sector S 600 plate reader. Phosphorylated STAT3 levels (i.e., raw MSD plate reads) were plotted vs IL-23 concentration in GraphPad Prism. The EC50 value for IL-23-induced STAT3 phosphorylation was calculated in GraphPad Prism using non-linear regression (curve fit) – [inhibitor] vs response (four-parameters) – robust regression. [00472] An initial set of phage display-derived anti-IL-23R mAbs was tested for detection of IL-23R on the surface of primary immune cells by staining PBMCs that had been stimulated for 4 days with anti-CD3 in the presence of IL-1β, conditions that induce IL-23 responsiveness and by extension, IL-23R expression. [00473] Surface IL-23R staining. For flow cytometric detection of IL-23R, up to ~10 6 cells were incubated in 50-100 µL Dulbecco’s phosphate buffered saline (PBS) supplemented with 0.2% bovine serum albumin (BSA) or FACS staining buffer with BSA (BD Pharmingen cat# 554657) supplemented with FcR blocking reagent (Miltenyi Biotec cat# 130-059-901) and Ghost dye red 780 (Tonbo Biosciences cat# 13-0865-T100). Following a 5-minute incubation on ice, 50 µL FACS staining buffer containing 20-30 µg/mL anti-IL-23R mAb were added to each sample such that the final concentration of antibody was 10 µg/mL. Cells were incubated for 60 minutes on ice and washed with FACS staining buffer. Cell pellets were resuspended in 100 µL FACS staining buffer containing biotinylated anti-mouse IgG 2a secondary antibody (BD Pharmingen cat# 550332) and incubated for 30 minutes on ice. After a second wash, cells were incubated in 100 µL FACS staining buffer containing streptavidin (SAV)-PE (BD Pharmingen cat# 349023 or Biolegend cat# 405203) and fluorescently labeled antibodies against relevant cell surface markers (Miltenyi Biotec and BD Pharmingen). Cells were acquired on a BD FACSCanto or FACSymphony cell analyzer, and data were analyzed using FlowJo software. [00474] To amplify the IL-23R signal, a three-step staining strategy was employed in which bound anti-IL-23R was detected with a biotinylated anti-mouse IgG 2a secondary antibody and streptavidin-PE. To establish a ‘cut-off’ for anti-IL-23R mAb binding, cells were incubated with buffer alone or the negative control mAb, I23RB5, during the first step of the three-step staining protocol. As an additional control, the biotinylated anti-mouse IgG 2a secondary reagent was omitted from the second staining step. [00475] As shown in FIG.4, the omission of either the primary or second step antibodies as well as three-step staining with I23RB5 resulted in low or no background staining on CD8 + and CD8- CD3 + CD56- T cells and CD3- CD56 + cells, respectively. A moderate level of nonspecific SAV-PE binding was detected on the surface of CD3 + CD56 + cells (FIG.4). The phage display-derived anti-IL- 23R mAbs I23RB1, I23RB2, I23RB3, I23RB4, and I23RB7 bound CD8 + and CD8- CD3 + CD56- T cells (FIG.5, part A) and a small but detectable number of CD3- CD56 + cells (FIG.5, part C). A majority of CD3 + CD56 + cells was stained with each phage display-derived anti-IL-23R mAb evaluated (FIG.5, part B). [00476] Two additional sets of anti-IL-23R mAbs derived from immunizing mice with the extracellular domain of human IL-23R were tested as described above for flow cytometric detection of IL-23R on the surface of primary human immune cells. Of 26 mouse immunization-derived mAbs tested, 22 bound CD8 + and CD8- CD3 + CD56- T cells to varying degrees including I23RB42, I23RB32, I23RB33, I23RB47, I23RB65, I23RB92, I23RB94, I23RB76, I23RB35, I23RB36, I23RB45, I23RB77, I23RB78, I23RB83, I23RB85, I23RB148, I23RB153, I23RB155, I23RB156, I23RB168, I23RB269, and I23RB313 (representative data shown in FIG.6). Of the immunization- derived mAbs, only I23RB76 gave equivalent (or improved) signal-to-noise relative to I23RB1, I23RB3, and I23RB4, the strongest cell binders among the previously identified phage display- derived mAbs. Notably, these four mAbs compete for binding to the IL-23R extracellular domain and thus, belong to the same ‘epitope bin.’ Example 4: Confirmation of IL-23R mAb binding specificity by siRNA-mediated IL23R knock- down [00477] To confirm the specificity of the anti-IL-23R mAbs for IL-23R, PBMCs that had been stimulated for 3 days with anti-CD3 and IL-1β were electroporated with a mixture of siRNA targeting the IL23R transcript. Following electroporation, the cells were placed back into culture on anti-CD3-coated flasks for ~24 hours, at which time the cells were pelleted for RNA isolation or stained for surface IL-23R and IL-12Rβ1 expression. [00478] siRNA-mediated IL23R knock-down. PBMCs were cultured on anti-CD3-coated flasks in serum-free medium supplemented with 100 ng/mL IL-1β. On day 3 of culture, ~10 7 cells were resuspended in 200 µL electroporation buffer provided with the P3 Primary Cell 4D- Nucleofector X Kit S (Lonza cat# V4XP-3032). A mixture of three siRNA molecules targeting the IL23R gene (Thermo Fisher Scientific cat# AM16708 assay ID 110064, 110065, 110066) or a negative control siRNA (Thermo Fisher Scientific cat# AM4611) was added to the cells such that the final concentration of siRNA was 300 nM (100 nM of each individual IL23R siRNA or 300 nM of the negative control siRNA). Following electroporation, the cells were placed back into anti-CD3-coated flasks and cultured for an additional ~24 hours. At that time, cells were stained for surface IL-23R and IL-12Rβ1 expression or pelleted for RNA isolation (Qiagen cat# 74004). Isolated RNA was reverse transcribed into cDNA (Applied Biosystems cat# 4374967) and IL23R and IL12RB1 transcript levels were analyzed by quantitative polymerase chain reaction (qPCR) (Thermo Fisher Scientific cat# 4304437) using probes for IL23R (Hs00332759_m1), IL12RB1 (Hs01106578_m1), ACTB (Hs99999903_m1), B2M (Hs00187842_m1), GAPDH (Hs02786624_g1), and HPRT1 (Hs02800695_m1). [00479] siRNA-mediated IL23R knock-down resulted in a ~1.9 to 38-fold reduction in IL23R transcript levels compared with cells electroporated with a negative control siRNA (FIG.7, part A). Transcript levels of IL12RB1 were either reduced or increased by IL23R knock-down depending on the housekeeping gene used for normalization (FIG.7, part A). [00480] Relative to cells electroporated with negative control siRNA, IL23R knock-down reduced I23RB4, I23RB7, and I23RB76 binding to CD4 + and CD8 + CD3 + CD56- T cells (FIG.7, parts B and C). Cells electroporated with IL23R or control siRNA expressed equivalent surface levels of IL-12Rβ1 (FIG.7, part D). Thus, I23RB4, I23RB7, and I23RB76 specifically detect IL-23R on the surface of primary human CD3 + CD56- T cells. Example 5: Antibody cross-reactive binding to Rat IL-23R [00481] Rat IL-23R cross-reactive binding was demonstrated in seven anti-human IL-23R antibodies that fall into several epitope bins, particularly falling into distinct epitope bins. Cross reactive binding is important and useful for application of the IL-23R antibodies in rats in vivo, ex vivo or in vitro (flow or other) studies without needing to generate specific anti-rat IL-23R surrogate antibodies with properties that approximately match those of any particular anti-human IL-23R mAb of interest. The generation of such surrogate mAbs can often be very challenging and require as much or even more work than that which was required to generate the initial human IL-23R antibodies. For these reasons, the anti-human IL-23R antibodies with rat IL-23R cross-reactive binding are of particular value. [00482] Table 13 below is modified from Tables 10 and 11 to indicate the antibody epitope binning results and also focus on the human and rat IL-23R binding of antibodies that demonstrated rat IL-23R binding. Antibody binding characteristics as available for antibodies in each of the epitope bins is provided. Antibodies in each of Bins 1, 5, 7, and 9 and also not binned antibodies I23RB30 and I23RB56 demonstrate rat IL-23R binding. Antibodies I23RB30 and I23RB56 have not been epitope binned due to not meeting criteria used to include mAbs in the epitope binning experiments. This view of the binding information shows that two of these mAbs (I23RB7, I23RB153) are the only mAb in their respective epitope bins (#5, #7). Two mAbs (I23RB42, I23RB157) fall within the same bin (Bin 1). Bin 1 contains a third mAb (I23RB85) which did not demonstrate rat IL-23R cross-reactivity in these studies, but which is predicted to bind rat IL-23R. A mAb within Bin 1 would be expected to be rat cross-reactive based on the phenotype of the other Bin 1 mAbs. This lack of rat IL-23R binding by I23RB85 in the studies can be plausibly explained in a couple of possible ways. I23RB85 was assessed for rat IL-23R binding using non-purified protein in expression culture supernatant. In this form, the amount of antibody could be lower than estimated and therefore be at a concentration that does not allow detection of binding. This is observed with I23RB42, which shows rat IL-23R binding when using purified protein but not when using non-purified protein in expression supernatant (Table 10). Also, I23RB85 could have lower affinity for rat IL-23R than for human IL-23R and with that lower affinity, not show detectable binding under the experimental conditions used in the binding studies. I23RB7 is an example of a mAb with lower affinity to rat IL-23R than to human IL-23R. The rat cross-reactive mAb I23RB45 falls into another distinct epitope bin (9). Epitope Bin 9 contains a second mAb, I23RB318, which does not show binding to rat IL-23R. This lack of rat IL-23R binding, which would be unexpected, can be explained in the same was as is explained above for I23RB85. [00483] Thus, overall, the following nine IL-23R antibodies have been shown to bind and/or are predicted to bind to rat IL-23R, based on rat binding studies and epitope binning: I23RB42, I23RB85, I23RB157, I23RB7, I23RB153, I23RB45, I23RB318, I23RB30 and I23RB56. TABLE 13. Epitope binning and rat IL-23R binding of human IL-23R binding mAbs
Example 6: Antibody CDR and Variable Region Sequences [00484] Tables 4-6 and 7-9 provide Heavy chain (HC), light chain (LC), variable region heavy chain (VH) and light chain (VL) and heavy and light chain CDR sequences for the IL-23R antibodies described and provided herein. Antibody fragments, particularly active or functional fragments or antigen binding fragments, may include or comprise the respective CDR sequences or the VH or VL sequence or the HC or LC sequence of the antibodies disclosed herein, or portions thereof. A review of the sequences identifies antibodies with related, similar or identical sequences. Antibodies are below designated in five groupings, wherein the antibodies have identical LC, VH and light chain CDR1, CDR2 and CDR3 sequences. In each instance, however, the antibodies have distinct or unque HC, VH and heavy chain CDR1, CDR2 and CDR3 sequences. [00485] For instance, some antibodies share light chain CDRs, and also may share LC and/or VL sequence. Notably these antibodies are distinct and unique in heavy chain sequence, including heavy chain CDRs and HC and VH sequences. The heavy chain sequences, including particularly the CDR sequences provided in and for these antibodies, are particularly responsible for binding differences or characteristics of these antibodies. Some bin together in the same epitope bin, while some are in distinct epitope bins or are uncharacterized by the bin analysis conducted. The below Table 13 identifies shared consensus light chain LC amino acid sequences and the corresponding IL- 23R antibodies comprising the LC sequence. Table 14 identifies shared consensus VL sequences and the corresponding IL-23R antibodies comprising the VL sequence. Table 14 identifies shared consensus light chain CDR1, CDR2 and CDR3 sequences and the corresponding IL-23R antibodies comprising the CDR sequences. Table 13 – Shared Antibody LC Amino Acid Sequences
Table 14 – Shared Antibody VL Amino Acid Sequences
Table 15 – Shared Antibody Light Chain CDR1, CDR2 and CDR3 Amino Acid Sequences
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